Relevant bibliographies by topics / RNA exosome

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Academic literature on the topic 'RNA exosome'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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Journal articles on the topic "RNA exosome"

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Crossland, Rachel E., Jean Norden, Louis Bibby, Joanna Davis, and Anne M. Dickinson. "Validation of Isolation Methodology and Endogenous Control Selection for qRT-PCR Assessment of Microrna Expression in Serum and Urine Exosomes." Blood 124, no. 21 (December 6, 2014): 5793. http://dx.doi.org/10.1182/blood.v124.21.5793.5793.

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Abstract Introduction: MicroRNAs are short RNA molecules that control ~50% of genes by binding to the mRNA 3’ UTR and repressing translation. Recently, they have been detected within exosomes; small vesicles secreted by most cells and abundant in body fluids. Exosomes are highly enriched for specific microRNAs and have been proposed as the starting point for circulating biomarker studies. To increase the accuracy of microRNA assessment by qRT-PCR, endogenous controls are required to correct for variability factors. Exosomal microRNA studies can be problematic, as endogenous controls previously used in cellular samples may not be present. This study compared exosome isolation and RNA extraction methods from urine and serum samples and identified suitable endogenous controls for incorporation into qRT-PCR analysis. Methods and Results: For serum exosomes, specialist isolation reagents from System Biosciences (SBI) (ExoQuick Serum Exosome Precipitation Solution) and Life Technologies (Total Exosome Isolation Reagent) were compared, followed by RNA extraction (Norgen Biotek Total RNA Purification kit) and qRT-PCR assessment of 3 endogenous controls (HY3, RNU48 & U6). Superior exosomal RNA recovery was achieved using Life Technologies reagent, demonstrated by higher RNA concentration (Life Technologies ng/ul 4.4, 7.5 & 6.9 vs. SBI ng/ul 3.8, 5.0 & 2.7) and lower endogenous control Ct values (HY3: Life Technologies 25.56, 28.54 & 26.69 vs. SBI 27.48, 30.48 & 35.36. RNU48: Life Technologies 30.95, undetected & 34.45 vs. SBI 30.95, undetected & undetected. U6: Life Technologies 21.83, 24.72 & 22.59 vs. SBI 21.59, 27.55 & 32.71, respectively). Recovery of exosomes (30-150 nm) was verified by electron microscopy. Serum exosomal RNA recovery was further assessed by isolating exosomes then comparing three commercially available RNA extraction kits (SBI SeraMir Exosome RNA Purification Column kit, Norgen Biotek Total RNA Purification kit & Qiagen RNeasy Micro kit). The Norgen Biotek kit gave the highest RNA yield (SBI ng/ul 13.0, 10.9 & 6.7 vs. Norgen ng/ul 23.2, 22.6 & 33.2 vs. Qiagen ng/ul 0.3, 0.6 & 0.4) and expression of two endogenous controls (HY3 & U6) (HY3: Norgen 26.76, 29.37 & 27.66 vs. SBI 31.45, 29.43 & 33.38 vs. Qiagen 35.00, 35.12 & 33.99. U6: Norgen 21.38, 24.96 & 21.31 vs. SBI 25.95, 24.91 & 30.17 vs. Qiagen 26.48, 27.14 & 27.39). In each case, exosomal isolation was confirmed by electron microscopy. To validate the methodology to isolate urine exosomal RNA, a commercially available kit was compared to ultracentrifugation. The Urine Exosome RNA Isolation kit (Norgen Biotek) gave superior results compared to ultracentrifugation followed by RNA extraction using the Norgen Biotek Total RNA Purification kit. This was demonstrated by higher RNA quantity (Norgen ng/ul 6.6, 6.4 & 11.5 vs. ultracentrifugation ng/ul 3.3, 4.5 & 2.9) and endogenous control (HY3 & U6) expression (HY3: Norgen 25.31, 26.33 & 26.85 vs. ultracentrifugation 31.54, 29.21 & 29.36. U6: Norgen 31.66, 30.83 & 33.47 vs. ultracentrifugation 32.49, 33.46 & 33.30). Exosomes isolated by the Norgen kit were also visualised by electron microscopy for further validation. The stability of 8 endogenous controls (RNU6B, RNU19, RNU38B, RNU43, RNU48, HY3, U6 & miR-320) was assessed by qRT-PCR in a test serum (n=10) and urine (n=15) exosome cohort from healthy controls and hematopoietic stem cell transplantation (HSCT) patients. HY3 and U6 were selected as the optimal controls for serum exosome miRNA expression analysis, with the highest level of stability across the panel (HY3: S.D 1.77 & CoV 6.2%, U6: S.D 2.14 & CoV 8.6%). HY3 and RNU48 were selected as the optimal controls for urine exosome miRNA expression analysis panel (HY3: S.D 1.67 & CoV 6.4%, RNU48: S.D 1.85 & CoV 5.3%). Selected optimal controls were analysed in a clinical HSCT serum (n=55) and urine (n=50) cohort. Expression stability was acceptable for all controls (serum U6: S.D 2.93 & CoV 11.8%. HY3: S.D 2.22 & CoV 7.4%. Urine RNU48: S.D 2.26 & CoV 6.9%, HY3: S.D 2.42 & CoV 8.8%), indicating constitutive expression in clinical samples. Conclusions: Exosomal microRNA studies are in their infancy and the number of commercially available exosome and RNA isolation kits are increasing. This study identifies the optimal methods to isolate serum and urine exosomal RNA as well as suitable endogenous controls for incorporation into qRT-PCR studies. Disclosures No relevant conflicts of interest to declare.
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Liu, Keda, Nanjue Cao, Yuhe Zhu, and Wei Wang. "Exosome: A Novel Nanocarrier Delivering Noncoding RNA for Bone Tissue Engineering." Journal of Nanomaterials 2020 (August 14, 2020): 1–14. http://dx.doi.org/10.1155/2020/2187169.

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Bone growth and metabolism are mainly regulated by a series of intracellular molecules and extracellular stimuli. Exosome, as a nanoscale substance secreted to the outside of the cells, plays an extensive role in intercellular communication. This review provides theoretical references and evidences for further exploration of exosomes as noncoding RNA carriers to regulate bone tissue recovery through the following aspects: (1) basic characteristics of exosomes, (2) research progress of exosomal noncoding RNA in bone tissue engineering, (3) current status and advantages of engineering exosomes as nanocarriers for noncoding RNA delivery, and (4) problems and application prospects of exosome therapy in the field of orthopedics.
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Mańka, Rafał, Pawel Janas, Karolina Sapoń, Teresa Janas, and Tadeusz Janas. "Role of RNA Motifs in RNA Interaction with Membrane Lipid Rafts: Implications for Therapeutic Applications of Exosomal RNAs." International Journal of Molecular Sciences 22, no. 17 (August 30, 2021): 9416. http://dx.doi.org/10.3390/ijms22179416.

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RNA motifs may promote interactions with exosomes (EXO-motifs) and lipid rafts (RAFT-motifs) that are enriched in exosomal membranes. These interactions can promote selective RNA loading into exosomes. We quantified the affinity between RNA aptamers containing various EXO- and RAFT-motifs and membrane lipid rafts in a liposome model of exosomes by determining the dissociation constants. Analysis of the secondary structure of RNA molecules provided data about the possible location of EXO- and RAFT-motifs within the RNA structure. The affinity of RNAs containing RAFT-motifs (UUGU, UCCC, CUCC, CCCU) and some EXO-motifs (CCCU, UCCU) to rafted liposomes is higher in comparison to aptamers without these motifs, suggesting direct RNA-exosome interaction. We have confirmed these results through the determination of the dissociation constant values of exosome-RNA aptamer complexes. RNAs containing EXO-motifs GGAG or UGAG have substantially lower affinity to lipid rafts, suggesting indirect RNA-exosome interaction via RNA binding proteins. Bioinformatics analysis revealed RNA aptamers containing both raft- and miRNA-binding motifs and involvement of raft-binding motifs UCCCU and CUCCC. A strategy is proposed for using functional RNA aptamers (fRNAa) containing both RAFT-motif and a therapeutic motif (e.g., miRNA inhibitor) to selectively introduce RNAs into exosomes for fRNAa delivery to target cells for personalized therapy.
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Sasaki, Reina, Tatsuo Kanda, Osamu Yokosuka, Naoya Kato, Shunichi Matsuoka, and Mitsuhiko Moriyama. "Exosomes and Hepatocellular Carcinoma: From Bench to Bedside." International Journal of Molecular Sciences 20, no. 6 (March 20, 2019): 1406. http://dx.doi.org/10.3390/ijms20061406.

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As hepatocellular carcinoma (HCC) usually occurs in the background of cirrhosis, which is an end-stage form of liver diseases, treatment options for advanced HCC are limited, due to poor liver function. The exosome is a nanometer-sized membrane vesicle structure that originates from the endosome. Exosome-mediated transfer of proteins, DNAs and various forms of RNA, such as microRNA (miRNA), long noncoding RNA (lncRNA) and messenger RNA (mRNA), contributes to the development of HCC. Exosomes mediate communication between both HCC and non-HCC cells involved in tumor-associated cells, and several molecules are implicated in exosome biogenesis. Exosomes may be potential diagnostic biomarkers for early-stage HCC. Exosomal proteins, miRNAs and lncRNAs could provide new biomarker information for HCC. Exosomes are also potential targets for the treatment of HCC. Notably, further efforts are required in this field. We reviewed recent literature and demonstrated how useful exosomes are for diagnosing patients with HCC, treating patients with HCC and predicting the prognosis of HCC patients.
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Zhou, Cuiqi, Stephen Shen, Rosemary Moran, and Shlomo Melmed. "Pituitary Somatotroph Adenoma Cell-Derived Exosomes: Characterization of Novel Non-Hormonal Functions." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A652—A653. http://dx.doi.org/10.1210/jendso/bvab048.1331.

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Abstract Exosomes, small extracellular vesicles carrying lipids, proteins, DNA and RNA, enable intercellular communication. Pituitary-derived exosomes have not been well validated, and as no human pituitary cell lines are available, we characterized exosomes derived from rat somatotroph tumor cells (GH1 and GH3). Rat FR and H9C2 cells were used as non-pituitary controls. Exosomes were isolated from serum-free culture supernatants by combining ultrafiltration and ultracentrifugation to eliminate hormone contamination. Derived exosomes were analyzed by NanoSight to visualize, size, and count particles. Exosomal proteins were extracted and exosome markers including TSG101, ALIX, CD63, HSP70, HSP90 detected by Western Blot. The exosome inhibitor GW4869 (10 µM, 30 h) reduced exosome release (up to 81%), whereas treating cells with hydrocortisone (0.1 µM, 72 h) increased exosome production (up to 42%) in GH1 and GH3 cells. Exosomal shuttle RNA characterized by RNA-Seq showed distinct pituitary vs non-pituitary exosome RNA profiles. Selected miRNAs assessed in exosomes and corresponding cells by qRT-PCR validated exosomal RNA-seq and suggested that miRNA signatures in exosomes and in respective cells of origin were concordant. Next, we explored downstream signaling of GH1-derived exosomes (GH1-exo) in vitro and in vivo and studied biological actions in normal hepatocytes and in malignant cells. As evidenced by mRNA-seq, GH1-exo distinctly altered signaling pathways in rat primary hepatocytes, vs pathways elicited by GH or PRL (0.5 µg/mL, 24 h). GH1-exo, FR-exo or vehicle were intravenously injected to 4-week-old female Wistar rats twice weekly for 4 weeks (5*109 exo/200 g, n=3), and livers dissected for mRNA-seq. Among GH1-exo specifically regulated genes, EIF2AK/ATF4, involved in cAMP responses and amino acid biosynthesis, were attenuated. In hepatocytes, GH1-exo suppressed up to 65% of nascent protein synthesis and reduced forskolin (10 µM)-stimulated cAMP activity by 19%, while GH (0.01-1 µg/mL) did not affect this pathway. Notably, GH1-exo also attenuated malignant cell motility. Both GH1-exo incubation or GH1 cell co-culture (48 h) suppressed migration, invasion and wound healing of HCT116 cancer cells by up to 70%. In contrast, treatment with rGH (0.5 µg/mL) increased HCT116 motility. Intravenous administration of GH1-exo (1010 exo/mouse, twice a week for 5 weeks) decreased metastatic tumor volume by 40% in nude mice harboring splenic HCT116 implants (5*105 cells/mouse, n=10), and especially abrogated hepatic metastases. mRNA-seq of GH1-exo treated HCT116 cells vs controls indicated dysregulated p53 and MAPK pathways, which may partially explain mechanisms underlying motility attenuation. The results elucidate novel biological actions of somatotroph adenoma cell-derived exosomes and suggest exosomes as non-hormonal messengers produced by pituitary tumors.
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Schageman, Jeoffrey, Emily Zeringer, Mu Li, Tim Barta, Kristi Lea, Jian Gu, Susan Magdaleno, Robert Setterquist, and Alexander V. Vlassov. "The Complete Exosome Workflow Solution: From Isolation to Characterization of RNA Cargo." BioMed Research International 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/253957.

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Exosomes are small (30–150 nm) vesicles containing unique RNA and protein cargo, secreted by all cell types in culture. They are also found in abundance in body fluids including blood, saliva, and urine. At the moment, the mechanism of exosome formation, the makeup of the cargo, biological pathways, and resulting functions are incompletely understood. One of their most intriguing roles is intercellular communication—exosomes function as the messengers, delivering various effector or signaling macromolecules between specific cells. There is an exponentially growing need to dissect structure and the function of exosomes and utilize them for development of minimally invasive diagnostics and therapeutics. Critical to further our understanding of exosomes is the development of reagents, tools, and protocols for their isolation, characterization, and analysis of their RNA and protein contents. Here we describe a complete exosome workflow solution, starting from fast and efficient extraction of exosomes from cell culture media and serum to isolation of RNA followed by characterization of exosomal RNA content using qRT-PCR and next-generation sequencing techniques. Effectiveness of this workflow is exemplified by analysis of the RNA content of exosomes derived from HeLa cell culture media and human serum, using Ion Torrent PGM as a sequencing platform.
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Morton, Derrick J., Emily G. Kuiper, Stephanie K. Jones, Sara W. Leung, Anita H. Corbett, and Milo B. Fasken. "The RNA exosome and RNA exosome-linked disease." RNA 24, no. 2 (November 1, 2017): 127–42. http://dx.doi.org/10.1261/rna.064626.117.

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Zhang, Liying, Yichen Ju, Si Chen, and Linzhu Ren. "Recent Progress on Exosomes in RNA Virus Infection." Viruses 13, no. 2 (February 8, 2021): 256. http://dx.doi.org/10.3390/v13020256.

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Recent research indicates that most tissue and cell types can secrete and release membrane-enclosed small vesicles, known as exosomes, whose content reflects the physiological/pathological state of the cells from which they originate. These exosomes participate in the communication and cell-to-cell transfer of biologically active proteins, lipids, and nucleic acids. Studies of RNA viruses have demonstrated that exosomes release regulatory factors from infected cells and deliver other functional host genetic elements to neighboring cells, and these functions are involved in the infection process and modulate the cellular responses. This review provides an overview of the biogenesis, composition, and some of the most striking functions of exosome secretion and identifies physiological/pathological areas in need of further research. While initial indications suggest that exosome-mediated pathways operate in vivo, the exosome mechanisms involved in the related effects still need to be clarified. The current review focuses on the role of exosomes in RNA virus infections, with an emphasis on the potential contributions of exosomes to pathogenesis.
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Sinha, Dona, Sraddhya Roy, Priyanka Saha, Nabanita Chatterjee, and Anupam Bishayee. "Trends in Research on Exosomes in Cancer Progression and Anticancer Therapy." Cancers 13, no. 2 (January 17, 2021): 326. http://dx.doi.org/10.3390/cancers13020326.

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Exosomes, the endosome-derived bilayered extracellular nanovesicles with their contribution in many aspects of cancer biology, have become one of the prime foci of research. Exosomes derived from various cells carry cargoes similar to their originator cells and their mode of generation is different compared to other extracellular vesicles. This review has tried to cover all aspects of exosome biogenesis, including cargo, Rab-dependent and Rab-independent secretion of endosomes and exosomal internalization. The bioactive molecules of the tumor-derived exosomes, by virtue of their ubiquitous presence and small size, can migrate to distal parts and propagate oncogenic signaling and epigenetic regulation, modulate tumor microenvironment and facilitate immune escape, tumor progression and drug resistance responsible for cancer progression. Strategies improvised against tumor-derived exosomes include suppression of exosome uptake, modulation of exosomal cargo and removal of exosomes. Apart from the protumorigenic role, exosomal cargoes have been selectively manipulated for diagnosis, immune therapy, vaccine development, RNA therapy, stem cell therapy, drug delivery and reversal of chemoresistance against cancer. However, several challenges, including in-depth knowledge of exosome biogenesis and protein sorting, perfect and pure isolation of exosomes, large-scale production, better loading efficiency, and targeted delivery of exosomes, have to be confronted before the successful implementation of exosomes becomes possible for the diagnosis and therapy of cancer.
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Makino, Debora Lika, and Elena Conti. "Structure determination of an 11-subunit exosome in complex with RNA by molecular replacement." Acta Crystallographica Section D Biological Crystallography 69, no. 11 (October 12, 2013): 2226–35. http://dx.doi.org/10.1107/s0907444913011438.

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The RNA exosome is an evolutionarily conserved multi-protein complex involved in the 3′ degradation of a variety of RNA transcripts. In the nucleus, the exosome participates in the maturation of structured RNAs, in the surveillance of pre-mRNAs and in the decay of a variety of noncoding transcripts. In the cytoplasm, the exosome degrades mRNAs in constitutive and regulated turnover pathways. Several structures of subcomplexes of eukaryotic exosomes or related prokaryotic exosome-like complexes are known, but how the complete assembly is organized to fulfil processive RNA degradation has been unclear. An atomic snapshot of aSaccharomyces cerevisiae420 kDa exosome complex bound to an RNA substrate in the pre-cleavage state of a hydrolytic reaction has been determined. Here, the crystallographic steps towards the structural elucidation, which was carried out by molecular replacement, are presented.
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More sources

Dissertations / Theses on the topic "RNA exosome"

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Giacometti, Simone. "CBC bound proteins and RNA fate." Thesis, Montpellier, 2016. http://www.theses.fr/2016MONTS028.

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Le complexe de liaison de la coiffe des ARN (CBC) joue un rôle essentiel dans leur maturation et déclenche une variété de réactions biochimiques, via son interaction avec différents partenaires. Deux complexes, CBC-ARS2-PHAX (CBCAP), et CBC-ARS2-ZC3H18-NEXT (CBCN), ont récemment été montré comme important pour cibler les ARN vers l'export (CBCAP) ou la dégradation (CBCN). Cependant, les mécanismes par lesquels la sélection se fait pour l'une voie ou l'autre reste mystérieuse. Ainsi, une question majeure qui reste à résoudre est de savoir quand et comment ces complexes sont recrutés sur les ARN. Dans ce travail, j'ai utilisé la procédure du iCLIP (Cross-Linking and Immuno-Precipitation), afin d'identifier les cibles de ces complexes sur l'ensemble du transcriptome humain. J'ai réalisé un iCLIP sur cinq composants de CBCAP et CBCN, et j'ai comparé les résultats à ceux obtenus avec RBM7, un composant de NEXT précédemment étudié par iCLIP. Mes résultats indiquent que: (i) CBP20, ARS2, PHAX et ZC3H18 se lient près de la coiffe des ARN, tandis que RBM7 et MTR4 se lient partout; (ii) CBP20, ARS2, PHAX et ZC3H18 s'associent à un large ensemble d'ARN transcrits par l'ARN polymérase II et montrent une faible sélectivité; (iii) la liaison de ces protéines varie avec l'état de maturation des ARN, avec le CBC enrichi sur les ARN matures, tout comme ARS2/PHAX/ZC3H18 et MTR4 (bien que dans une moindre mesure), tandis que RBM7 est préférentiellement lié sur les pre-mRNAs non épissés; (iv) une liaison différentielle de RBM7 et MTR4 sur les ARN, avec RBM7 enrichi sur les introns et les PROMPTs, et MTR4 plus présent sur les ARN mature. Bien que des expériences additionnelles soient requises, nous proposons que le CBCAP et le CBCN se lient à un même ensemble d'ARN, ce qui indique à la fois une compétition entre ZC3H18 et PHAX pour la liaison à ces ARN, et l'absence de voies de routage bien déterminées qui ciblerait les ARN vers l'une ou l'autre de ces protéines. Le devenir des ARN pourrait ainsi être déterminé par d'autres caractéristiques des ARN, ou encore par des protéines additionnelles. Ces facteurs pourraient s'allier aux protéines liées à la coiffe afin de favoriser la formation du CBCAP ou du CBCN. Dans le but d’identifier des facteurs additionnels, j'ai réalisé un screen d'interaction par spectrométrie de masse après purification de ARS2 ou CBP80. Ceci a été fait dans des conditions natives ou après un cross-link des complexes à la formaldéhyde, afin de stabiliser les interactions transitoires. Ceci a permis d'identifier de nouveaux partenaires de ARS2 et de CBP80, dont la majorité sont impliqués dans l'épissage des ARN. Des expériences additionnelles seront nécessaires pour valider ces interactions
The cap-binding complex (CBC) plays a pivotal role in post-transcriptional processing events and orchestrates a variety of metabolic pathways, through association with different interaction partners. Two CBC sub-complexes, the CBC-ARS2-PHAX (CBCAP) and the CBC-nuclear exosome targeting (NEXT) complex (CBCN), were recently shown to target capped RNA either toward export or degradation, but the mechanisms by which they can discriminate between different RNA families and route them toward different metabolic pathways still remain unclear. A major question to be answered is how and when the different CBC subcomplexes are recruited to the RNP. Here, we used an individual nucleotide-resolution UV cross-linking and immunoprecipitation (iCLIP) approach to identify the transcriptome-wide targets for 5 different components of the CBCAP and CBCN complexes, and compared results to the previously analysed NEXT-component RBM7. We report that: (i) CBP20, ARS2, PHAX and ZC3H18 bind close to the cap, while RBM7 and MTR4 bind throughout the mRNA body; (ii) CBP20, ARS2, PHAX and ZC3H18 associate with a broad set of RNA polymerase II (PolII)-derived RNAs and have only mild species preferences; (iii) binding varies with the RNA maturation stage, with the CBC being highly enriched on mature mRNA, ARS2/PHAX/ZC3H18/MTR4 less so, and RMB7 preferentially bound to pre-mRNAs; (iv) MTR4 and RBM7 show different specificities, with RBM7 being highly enriched on introns and promoter upstream transcripts (PROMPTs), while MTR4 is additionally present on mature RNAs. Although more experimental work is needed to fully support our model, we propose that CBCAP and CBCN bind overlapping sets of RNAs, indicating a competition between the proteins ZC3H18 and PHAX, and the lack of a strict RNA sorting mechanism. RNA fate may therefore be determined by additional RNA features and/or by other RNA-binding proteins, which may synergize with the cap and drive the formation of one specific CBC subcomplex instead of another. In an attempt to identify yet unknown factors that may interact with cap-bound CBCAP and CBCN, we performed a protein interaction screen leveraging affinity capture-mass spectrometry (ACMS), using ARS2 and CBP80 as bait proteins. As a complementary approach, we also employed a formaldehyde-based chemical cross-linking strategy, aimed at stabilizing weak/transient interactions. Although we failed to detect any transient interactions involving the CBC, we identified several potential CBC80 and ARS2 interactors, the majority of which are involved in pre-mRNA splicing. Additional quantitative experiments are required to validate our ACMS results and confirm the existence of such protein interactions in vivo
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Paiva, Germano Alves. "Estudo do papel de Rrp43p na montagem e estabilização do complexo do exossomo em Saccharomyces cerevisiae." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-09052013-105201/.

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O exossomo é um complexo constituído por até 11 subunidades (Rrp4p, Rrp6p, Rrp40p, Rrp41p, Rrp42p, Rrp43p, Rrp44p, Rrp45p, Rrp46p, Csl4p, Mtr3p) que possui atividade exorribonucleolítica 3`→5` e está envolvido no processamento e degradação de vários tipos de RNAs na célula eucariótica. O complexo tem sido estudado em diversos organismos, como leveduras, insetos, plantas, humanos e também em várias espécies de archaea. Apesar da conservação da estrutura do exossomo ao longo da evolução e de oito subunidades do exossomo eucariótico apresentarem domínios de RNase, apenas duas proteínas, Rrp6p e Rrp44p têm atividade catalítica. A despeito da importância do exossomo para a célula, ainda não está claro o papel de cada subunidade na atividade do complexo. Neste trabalho foram utilizados mutantes da subunidade Rrp43p a fim de avaliar como mutações pontuais nesta subunidade afetam a montagem e estabilização do complexo do exossomo de Saccharomyces cerevisiae. Ensaios de purificação do exossomo com TAP-Rrp43p revelaram que os mutantes co-purificam Mtr3p e Rrp44p menos eficientemente. Além disso, os mutantes também apresentam atividade exorribonucleolítica 3`→5` reduzida, indicando que o defeito na montagem do complexo pode afetar a sua atividade enzimática.
The exosome is a protein complex comprised of up to eleven subunits (Rrp4p, Rrp6p, Rrp40p, Rrp41p, Rrp42p, Rrp43p, Rrp44p, Rrp45p, Rrp46p, Csl4p and Mtr3p) that has 3`→5` exoribonucleolytic activity and is involved in degradation and processing pathways of several kinds of RNA in eukaryotes. This complex has also been identified in several organisms, such as yeast, insects, plants, humans and also many species of archaea. Despite the overall structure conservation of the complex throughout evolution and eight of the eukaryotic exosome subunits displaying RNase domains, only two proteins, Rrp6p and Rrp44p have catalytic activity. Although the exosome has been shown to be involved in many different aspects of RNA metabolism, the role that each subunit plays in the activity of the complex has not yet been determined. In this work we used of TAP-purified exosome complexes to study the effect of Rrp43p mutations on the assembly and stabilization of the complex in Saccharomyces cerevisiae. Co-immunoprecipitation assays revealed that Rrp43p mutants co-purify Mtr3p and Rrp44p subunits less efficiently. Besides, Rrp43p mutants also present decreased activity, indicating that an assembly defect may affect its enzymatic activity
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Kiss, Daniel L. "The Exozyme Model: A New Paradigm of Exosome Subunit Activity Revealed by Diverse and Distinct Substrate Specificities of Exosome Subunits In Vivo." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1263237977.

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Wlotzka, Wiebke. "RNA-protein crosslinking identifies novel targets for the nuclear RNA surveillance machinery." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/5047.

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The RNA binding proteins Nrd1 and Nab3 function in transcription termination by RNA Pol II, acting via interactions with the CTD of the largest polymerase subunit, particularly on snRNA and snoRNA genes. They also participate in nuclear RNA surveillance and ncRNA degradation, functioning together with the exosome and the Trf-Air-Mtr4 polyadenylation (TRAMP) complexes. To better understand the signals for surveillance and ncRNA degradation, I applied an RNA-protein crosslinking approach in combination with Solexa sequencing. This approach identified in vivo binding sites for Nrd1, Nab3 and Trf4. Several million sequences were recovered and mapped to the yeast genome. This identified three classes of substrates: 1) Expected targets, including snRNAs, snoRNAs and characterized short ncRNAs. 2) Unknown but anticipated substrates, including several hundred previously uncharacterized ncRNAs that lie antisense to protein coding genes (asRNAs). 3) Unexpected targets, including many Pol III transcribed precursor RNAs. Bioinformatics analyses of the high-throughput sequencing data revealed that known binding motifs for Nrd1 and Nab3 were frequently recovered. Many recovered RNAs contained non-templated oligo(A) tails with an average of 2-5 nt length. This clearly distinguishes targets for surveillance machinery from polyadenylated mRNAs that get stabilized by polyadenylation (A70-90 in yeast). For a few selected, predicted asRNAs I was able to validate the crosslinking data by demonstrating that corresponding long RNAs are both detectable and increased by loss of Nrd1, Nab3, Trf4 or the exosome component Rrp6. Interestingly, loss of Nrd1 or Nab3 led to transcriptional read through on long asRNA transcripts. In addition, I have identified pre-TLC1 (telomerase RNA) as a target for the surveillance machinery. Processing of this long ncRNA was only poorly characterized in yeast but I could demonstrate that its transcription termination and maturation is mainly dependent on actions of the Nrd1-Nab3-Sen1, TRAMP4 and exosome complexes. It was previously reported that Nrd1-Nab3 acts only on short RNAs, due to the association with Ser5 phosphorylated CTD. My findings suggest that action of Nrd1- Nab3 is not exclusively on Ser5 phosphorylated form of the CTD. Unexpectedly the Pol II associated factors Nrd1 and Nab3 bound Pol III precursor transcripts. Surveillance of Pol III transcripts was dependent on Nrd1 and Nab3 since depletion of Nrd1 or Nab3 led to accumulation of pre-tRNAs. In addition, I could demonstrate that pre-RNase P RNA is oligoadenylated in vivo, which was dependent on Nrd1, Nab3 and Trf4. Together, my findings suggest a revised model of nuclear RNA surveillance in which Nrd1-Nab3 not only acts in co-transcriptional RNA recognition on Pol II transcripts but also post-transcriptionally on Pol III RNAs. The TRAMP complex is recruited to the defective RNA by the Nrd1-Nab3 complex, which remains associated with the RNA through the process of polyadenylation, until the exosome degrades the aberrant transcript.
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Hessle, Viktoria. "Characterization of RNA exosome in Insect Cells : Role in mRNA Surveillance." Doctoral thesis, Stockholms universitet, Institutionen för molekylärbiologi och funktionsgenomik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-52127.

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The exosome, an evolutionarily conserved protein complex with exoribonucleolytic activity, is one of the key players in mRNA quality control. Little is known about the functions of the exosome in metazoans. We have studied the role of the exosome in nuclear mRNA surveillance using Chironomus tentans and Drosophila melanogaster as model systems. Studies of the exosome subunits Rrp4 and Rrp6 revealed that both proteins are associated with transcribed genes and nascent pre-mRNPs in C. tentans. We have shown that several exosome subunits interact in vivo with the mRNA-binding protein Hrp59/hnRNP M, and that depleting Hrp59 in D. melanogaster S2 cells by RNAi leads to reduced levels of Rrp4 at the transcription sites. Our results on Rrp4 suggest a model for cotranscriptional quality control in which the exosome is constantly recruited to nascent mRNAs through interactions with specific hnRNP proteins. Moreover, we show that Rrp6 interacts with mRNPs in transit from the gene to the nuclear pore complex, where it is released during early stages of nucleo-cytoplasmic translocation. Furthermore, we show that Rrp6 is enriched in discrete nuclear bodies in the salivary glands of C. tentans and D. melanogaster. In C. tentans, the Rrp6-rich nuclear bodies colocalize with SUMO. We have also constructed D. melanogaster S2 cells expressing human b-globin genes, with either wild type of mutated splice sites, and we have studied the mechanisms by which the cells react to pre-mRNA processing defects. Our results indicate that two surveillance responses operate co-transcriptionally in S2 cells. One requires Rrp6 and retains defective mRNAs at the transcription site. The other one reduces the synthesis of the defective transcripts through a mechanism that involves histone modifications. These observations support the view that multiple mechanisms contribute to co-transcriptional surveillance in insects.
At the time of the doctoral defense, the following paper was unpublished and had a status as follows: Paper 4: Manuscript.
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Witharana, Chamindri [Verfasser]. "The heterogeneity of the RNA degradation exosome in Sulfolobus solfataricus / Chamindri Witharana." Gießen : Universitätsbibliothek, 2013. http://d-nb.info/1065395418/34.

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Feigenbutz, Monika U. "Role of the exosome co-factor Rrp47 in RNA processing and surveillance." Thesis, University of Sheffield, 2013. http://etheses.whiterose.ac.uk/5285/.

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RNA surveillance by the exosome complex is remarkably conserved from yeast to humans and best studied in baker's yeast Saccharomyces cerevisiae. The multi-subunit RNA exosome is involved in the processing, maturation, quality control and general turnover of RNAs, as well as the degradation of harmful, aberrant or unwanted transcripts. To execute its distinct cytoplasmic and nuclear functions, the exosome requires compartment-specific co-factors like Rrp47, a protein directly associated with the nuclear exosome exoribonuclease Rrp6. The aim of this study was to investigate the role of Rrp47 in exosome-mediated processes based on the model that Rrp47 is an RNA binding protein that helps direct Rrp6 to its substrates. Mutational analysis of Rrp47 revealed that the Sas10 domain which Rrp47 shares with other proteins involved in RNA processing is critical for Rrp6 binding and for all in vivo Rrp47 functions. However, the less conserved C-terminus of Rrp47 functions in the final maturation of snoRNAs, and both C- and N-terminus cooperate in RNA binding in vitro. Protein and mRNA expression analyses demonstrate that the proteins critically influence each other's stability and expression levels whereby Rrp47 expression is drastically reduced when Rrp6 is absent. Studies into the assembly of Rrp47-Rrp6 suggest that the proteins are imported into the nucleus separately where Rrp47 is degraded if Rrp6 is not available for interaction. Rrp47 has less pronounced effects on Rrp6 stability and expression, yet defects in the processing of Nrd1 terminated transcripts were alleviated by Rrp6 overexpression in cells lacking Rrp47. Specifically, growth was restored by overexpressing Rrp6 in an otherwise synthetic lethal rex1? rrp47? strain, suggesting that Rrp47 is critical for maintaining adequate Rrp6 levels. Taken together this study has given crucial new insights into domains required for Rrp47 function, as well as assembly and interdependency of Rrp47 and its associated exonuclease Rrp6.
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Rege, Mayuri. "RNA Exosome & Chromatin: The Yin & Yang of Transcription: A Dissertation." eScholarship@UMMS, 2015. http://escholarship.umassmed.edu/gsbs_diss/812.

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Eukaryotic genomes can produce two types of transcripts: protein-coding and non-coding RNAs (ncRNAs). Cryptic ncRNA transcripts are bona fide RNA Pol II products that originate from bidirectional promoters, yet they are degraded by the RNA exosome. Such pervasive transcription is prevalent across eukaryotes, yet its regulation and function is poorly understood. We hypothesized that chromatin architecture at cryptic promoters may regulate ncRNA transcription. Nucleosomes that flank promoters are highly enriched in two histone marks: H3-K56Ac and the variant H2A.Z, which make nucleosomes highly dynamic. These histone modifications are present at a majority of promoters and their stereotypic pattern is conserved from yeast to mammals, suggesting their evolutionary importance. Although required for inducing a handful of genes, their contribution to steady-state transcription has remained elusive. In this work, we set out to understand if dynamic nucleosomes regulate cryptic transcription and how this is coordinated with the RNA exosome. Remarkably, we find that H3-K56Ac promotes RNA polymerase II occupancy at a large number of protein coding and noncoding loci, yet neither histone mark has a significant impact on steady state mRNA levels in budding yeast. Instead, broad effects of H3-K56Ac or H2A.Z on levels of both coding and ncRNAs are only revealed in the absence of the nuclear RNA exosome. We show that H2A.Z functions with H3-K56Ac in chromosome folding, facilitating formation of Chromosomal Interaction Domains (CIDs). Our study suggests that H2A.Z and H3-K56Ac work in concert with the RNA exosome to control mRNA and ncRNA levels, perhaps in part by regulating higher order chromatin structures. Together, these chromatin factors achieve a balance of RNA exosome activity (yin; negative) and Pol II (yang; positive) to maintain transcriptional homeostasis.
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Jackson, Ryan N. "Structural and Functional Characterization of the Essential RNA Helicase Mtr4." DigitalCommons@USU, 2012. https://digitalcommons.usu.edu/etd/1414.

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The essential protein Mtr4 is a conserved Ski2-like RNA helicase that maintains the integrity of nuclear RNA by promoting the 3' end decay of a wide variety of RNA substrates. Mtr4 activates the multi-protein exosome in RNA processing, surveillance, and turnover pathways by unwinding secondary structure and/or displacing associated proteins from RNA substrates. While Mtr4 may be able to promote decay independently, it is often associated with large multi-protein assemblies. Specifically, Mtr4 is the largest member of the TRAMP (Trf4/Air2/Mtr4 polyadenylation) complex which targets a plethora of RNA substrates for degradation by appending them with small (~5nt) poly(A) tails via the polymerase activity of Trf4. Mtr4 preferentially binds and unwinds RNAs with short poly(A) tails. Notably, the mechanism by which Mtr4 recognizes the length and identity of the RNA 3' end is coupled to the modulation of poly(A) polymerase activity of Trf4. The lack of structural data for Mtr4 and associated complexes severely limits the understanding of Mtr4 function. Particularly, it is unclear how Mtr4 senses RNA features, acts on RNA substrates, delivers RNA substrates to the exosome, and assembles into larger protein complexes. Presented here is the x-ray crystal structure of Mtr4 combined with detailed structural and biochemical analysis of the enzyme. The structure reveals that Mtr4 contains a four domain helicase core that is conserved in other RNA helicases and a unique arch-like RNA binding domain that is required for the in vivo processing of 5.8S rRNA. Furthermore, kinetic and in vivo analysis of conserved residues implicated in the poly(A) sensing mechanism demonstrates that ratchet helix residues regulate RNA unwinding and impact RNA sequence specificity. A comparison of the apo Mtr4 structure with the RNA/ADP bound structure (determined elsewhere) provides a view of the range of motion that individual domains of Mtr4 adopt upon substrate binding as well as the possible conformations that occur during RNA translocation. These studies provide an important framework for understanding the fundamental role of Mtr4 in exosome-mediated RNA decay, and more broadly describe common themes in architecture and function of the Ski2-like helicase family.
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Kong, Ka-yiu, and 江家耀. "Characterization of the roles of yeast nuclear exosome cofactor TRAMP complex in pre-mRNA splicing." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/193522.

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In budding yeast, the Trf4/5p-Air1/2p-Mtr4p polyadenylation (TRAMP) complex recognizes unwanted RNA transcripts in the nucleus and then targets them to the nuclear exosome for rapid degradation, constituting an important pathway of nuclear RNA quality control. Each pre-mRNA splicing event unavoidably generates a RNA side-product that should be recognized by TRAMP and then removed by the nuclear exosome to prevent the potentially harmful sequestration of splicing factors and/or ribonucleotides. While successful pre-mRNA splicing inevitably produces a spliced-out intron, errors in pre-mRNA splicing lead to the emergence of either an abnormal splicing intermediate, or a splicing-incompetent pre-mRNA that cannot be properly spliced. However, it remains unclear how and when these RNA side-products of pre-mRNA splicing are recognized by TRAMP. In this study, chromatin immunoprecipitation (ChIP) was applied to demonstrate that both TRAMP and the nuclear exosome component Rrp6p are cotranscriptionally recruited to nascent RNA transcripts, particularly to intronic sequences, indicating that splicing side-products are recognized by TRAMP and committed to subsequent nuclear-exosome-mediated degradation in a cotranscriptional manner. Deletion of TRF4, of both AIR1 and AIR2, or of RRP6, resulted in accumulation of unspliced pre-mRNAs. Surprisingly, while such pre-mRNAs accumulated in rrp6 cells owing to defects in pre-mRNA degradation, the same phenotype in trf4 and air1air2 cells involved splicing defects, demonstrating that only TRAMP, but not the nuclear exosome, contributes to optimal pre-mRNA splicing. Consistent with a direct stimulatory role for TRAMP in pre-mRNA splicing, negative genetic interactions and physical interactions between Trf4p and several splicing factors were observed, and that Trf4p was further shown to be required for optimal recruitment of the splicing factor Msl5p. The direct facilitation of pre-mRNA splicing by TRAMP may act as a fail-safe mechanism to ensure the cotranscriptional recruitment of TRAMP to nascent intron-containing transcripts before or during pre-mRNA splicing, such that the subsequently generated spliced-out introns, abnormal splicing intermediates, or splicing-incompetent pre-mRNAs can be recognized immediately by TRAMP, and then targeted to the nuclear exosome for prompt degradation before their potentially harmful accumulation. Since most TRAMP and nuclear exosome components found in budding yeast also contain functional human homologs, this work provides important insights into how splicing side-products are rapidly degraded by the nuclear RNA quality control system in human cells, which have a much higher frequency of introns within their genome, and certainly require a much more efficient pathway for the removal of an increased amount of splicing side-products due to the greater number of splicing events.
published_or_final_version
Biochemistry
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Doctor of Philosophy
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Books on the topic "RNA exosome"

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service), SpringerLink (Online, ed. RNA Exosome. New York, NY: Landes Bioscience and Springer Science+Business Media, LLC, 2010.

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Jensen, Torben Heick, ed. RNA Exosome. New York, NY: Springer US, 2010. http://dx.doi.org/10.1007/978-1-4419-7841-7.

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LaCava, John, and Štěpánka Vaňáčová, eds. The Eukaryotic RNA Exosome. New York, NY: Springer New York, 2020. http://dx.doi.org/10.1007/978-1-4939-9822-7.

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Jensen, Torben Heick. RNA Exosome. Springer, 2011.

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Kumar, Vinod, Pranela Rameshwar, and Karl L. Mettinger. Exosomes, Stem Cells and MicroRNA: Aging, Cancer and Age Related Disorders. Springer, 2018.

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Exosomes, Stem Cells and MicroRNA: Aging, Cancer and Age Related Disorders. Springer, 2018.

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Book chapters on the topic "RNA exosome"

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Delan-Forino, Clémentine, and David Tollervey. "Mapping Exosome–Substrate Interactions In Vivo by UV Cross-Linking." In Methods in Molecular Biology, 105–26. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_6.

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AbstractThe RNA exosome complex functions in both the accurate processing and rapid degradation of many classes of RNA in eukaryotes and Archaea. Functional and structural analyses indicate that RNA can either be threaded through the central channel of the exosome or more directly access the active sites of the ribonucleases Rrp44 and Rrp6, but in most cases, it remains unclear how many substrates follow each pathway in vivo. Here we describe the method for using an UV cross-linking technique termed CRAC to generate stringent, transcriptome-wide mapping of exosome–substrate interaction sites in vivo and at base-pair resolution.
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Fasken, Milo B., Derrick J. Morton, Emily G. Kuiper, Stephanie K. Jones, Sara W. Leung, and Anita H. Corbett. "The RNA Exosome and Human Disease." In Methods in Molecular Biology, 3–33. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_1.

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LaCava, John, and Štěpánka Vaňáčová. "Correction to: The Eukaryotic RNA Exosome." In Methods in Molecular Biology, C1—C4. New York, NY: Springer New York, 2020. http://dx.doi.org/10.1007/978-1-4939-9822-7_25.

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Cruz, Cristina, and Jonathan Houseley. "Protocols for Northern Analysis of Exosome Substrates and Other Noncoding RNAs." In Methods in Molecular Biology, 83–103. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_5.

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AbstractOver the past decade a plethora of noncoding RNAs (ncRNAs) have been identified, initiating an explosion in RNA research. Although RNA sequencing methods provide unsurpassed insights into ncRNA distribution and expression, detailed information on structure and processing are harder to extract from sequence data. In contrast, northern blotting methods provide uniquely detailed insights into complex RNA populations but are rarely employed outside specialist RNA research groups. Such techniques are generally considered difficult for nonspecialists, which is unfortunate as substantial technical advances in the past few decades have solved the major challenges. Here we present simple, reproducible and highly robust protocols for separating glyoxylated RNA on agarose gels and heat denatured RNA on polyacrylamide–urea gels using standard laboratory electrophoresis equipment. We also provide reliable transfer and hybridization protocols that do not require optimization for most applications. Together, these should allow any molecular biology lab to elucidate the structure and processing of ncRNAs of interest.
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Januszyk, Kurt, and Christopher D. Lima. "Reconstitution of the Schizosaccharomyces pombe RNA Exosome." In Methods in Molecular Biology, 449–65. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_22.

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Januszyk, Kurt, Eva-Maria Weick, and Christopher D. Lima. "Reconstitution of the Human Nuclear RNA Exosome." In Methods in Molecular Biology, 467–89. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_23.

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Marqués-García, Fernando, and María Isidoro-García. "Protocols for Exosome Isolation and RNA Profiling." In Methods in Molecular Biology, 153–67. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3652-6_11.

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Schmid, Manfred, and Torben Heick Jensen. "The Nuclear RNA Exosome and Its Cofactors." In Advances in Experimental Medicine and Biology, 113–32. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-31434-7_4.

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Taylor, Douglas D., Wolfgang Zacharias, and Cicek Gercel-Taylor. "Exosome Isolation for Proteomic Analyses and RNA Profiling." In Methods in Molecular Biology, 235–46. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-068-3_15.

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Lloret-Llinares, Marta, and Torben Heick Jensen. "Global Identification of Human Exosome Substrates Using RNA Interference and RNA Sequencing." In Methods in Molecular Biology, 127–45. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9822-7_7.

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Conference papers on the topic "RNA exosome"

1

Lu, Yunxing, Xiaoyu Jian, Zhaoduo Tong, Zhenhua Wu, Shihui Qiu, Chuanjie Shen, Hao Yin, and Hongju Mao. "Integrated On-Chip Cellular Exosome Isolation and RNA Analysis Microsystem." In 2021 21st International Conference on Solid-State Sensors, Actuators and Microsystems (Transducers). IEEE, 2021. http://dx.doi.org/10.1109/transducers50396.2021.9495727.

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Preet, Ranjan, Shufei Zhuang, Wei-Ting Hung, Lane K. Christenson, and Dan A. Dixon. "Abstract A41: The RNA binding protein HuR enhances exosome secretion in colorectal cancer." In Abstracts: AACR Special Conference: The Function of Tumor Microenvironment in Cancer Progression; January 7-10, 2016; San Diego, CA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.tme16-a41.

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Preet, Ranjan, Wei-Ting Hung, Shufei Zhuang, Lane K. Christenson, and Dan A. Dixon. "Abstract B05: The RNA-binding protein HuR enhances exosome secretion in colorectal cancer." In Abstracts: AACR Special Conference: Colorectal Cancer: From Initiation to Outcomes; September 17-20, 2016; Tampa, FL. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.crc16-b05.

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Sanz Rubio, D., A. R. Remacha, L. Pastor, P. Cubero, E. Vera, and J. M. Marin. "Micro-RNA Exosome Cargo from Induced Sputum: New Tool for Approaching Asthma Research." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7411.

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Preet, Ranjan, Shufei Zhuang, Wei-ting Hung, Lane K. Christenson, and Dan A. Dixon. "Abstract 5104: The RNA binding protein HuR enhances exosome secretion in colorectal cancer." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5104.

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Berrondo, Claudia, Jonathan Flax, Edward M. Messing, and Carla Beckham. "Abstract 152: The long non-coding RNA HOTAIR affects exosome-mediated bladder cancer progression." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-152.

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Skog, Johan, Mikkel Noerholm, Stefan Bentink, Charlotte Romain, Jillian Fishbeck, Ian Sinclair, Anna Scott, Romy Mueller, Tina Koestler, and Susan Belzer. "Abstract B34: Development of a urine microvesicle/exosome RNA biomarker panel to identify prostate cancer." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-b34.

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Huang, Y., T. Li, Z. Huang, W. Deng, S. Zheng, X. Guo, and Z. Huang. "THU0010 Altered mirnas profiles in plasma-derived exosome of patients with ankylosing spondylitis by small rna-seq analysis." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.5637.

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Francisco-Garcia, Ana, Rocio T. Martinez-Nunez, Hitasha Rupani, Laurie C. Lau, Peter H. Howarth, and Tilman Sanchez-Elsner. "LSC Abstract – Altered small RNA cargo in severe asthma exosomes." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pp101.

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Lovisa, F., E. Gaffo, C. Elia, A. Garbin, I. Gallingani, CC Damanti, E. Carraro, et al. "RNA-seq analysis of plasmatic exosomal miRNAs in pediatric Hodgkin Lymphoma." In ISCAYAHL 2020. © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1701810.

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Reports on the topic "RNA exosome"

1

Wu, Zilong, Zihao Xu, Boyao Yu, Jing tao Zhang, and Bentong Yu. The potential diagnostic value of exosomal long non-coding RNAs in solid tumours: a meta-analysis and systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, June 2020. http://dx.doi.org/10.37766/inplasy2020.6.0083.

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Testroet, Eric D., Sayane Shome, James M. Reecy, Robert L. Jernigan, Meijun Zhu, Min Du, Stephanie Clark, and Donald C. Beitz. Profiling of the Exosomal Cargo of Bovine Milk Reveals the Presence of Immune- and Growth-modulatory Non-coding RNAs (ncRNA). Ames (Iowa): Iowa State University, January 2018. http://dx.doi.org/10.31274/ans_air-180814-330.

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