Academic literature on the topic 'Piwi proteins'

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Journal articles on the topic "Piwi proteins"

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Wei, Bang-Hong, Jia-Hao Ni, Tong Yang, Shuang-Li Hao, and Wan-Xi Yang. "PIWIs maintain testis apoptosis to remove abnormal germ cells in Eriocheir sinensis." Reproduction 162, no. 3 (September 1, 2021): 193–207. http://dx.doi.org/10.1530/rep-21-0157.

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PIWI proteins play important roles in germline development in the mammals. However, the functions of PIWIs in crustaceans remain unknown. In the present study, we identified three Piwis from the testis of Eriocheir sinensis (E. sinensis). Three Piwi genes encoded proteins with typical features of PIWI subfamilies and were highly expressed in the testis. Three PIWIs could be detected in the cytoplasm of spermatocytes and spermatids, while in spermatozoa, we could only detect PIWI1 and PIWI3 in the nucleus. The knockdown of PIWIs by dsRNA significantly affected the formation of the nuclei in spermatozoa, which resulted in deviant and irregular nuclei. PIWI defects significantly inhibited the apoptosis of abnormal germ cells through the caspase-dependent apoptosis pathway and p53 pathway. Knockdown of PIWIs inhibited the expression of caspase (Casp) 3, 7, 8, and p53 without affecting Bcl2 (B-cell lymphoma gene 2), Bax (B-cell lymphoma-2-associated X), and BaxI (B-cell lymphoma-2-associated X inhibitor), which further significantly increased abnormal spermatozoa in the knockdown-group crabs. These results show a new role of PIWI proteins in crustaceans that is different from that in mammals. In summary, PIWIs play roles in the formation of the germline nucleus and can maintain apoptosis in abnormal germ cells to remove abnormal germ cells in E. sinensis.
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Wang, Chen, Zhen-Zhen Yang, Fang-Hao Guo, Shuo Shi, Xiao-Shuai Han, An Zeng, Haifan Lin, and Qing Jing. "Heat shock protein DNAJA1 stabilizes PIWI proteins to support regeneration and homeostasis of planarian Schmidtea mediterranea." Journal of Biological Chemistry 294, no. 25 (May 10, 2019): 9873–87. http://dx.doi.org/10.1074/jbc.ra118.004445.

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PIWI proteins are key regulators of germline and somatic stem cells throughout different evolutionary lineages. However, how PIWI proteins themselves are regulated remains largely unknown. To identify candidate proteins that interact with PIWI proteins and regulate their stability, here we established a yeast two-hybrid (Y2H) assay in the planarian species Schmidtea mediterranea. We show that DNAJA1, a heat shock protein 40 family member, interacts with the PIWI protein SMEDWI-2, as validated by the Y2H screen and co-immunoprecipitation assays. We found that DNAJA1 is enriched in planarian adult stem cells, the nervous system, and intestinal tissues. DNAJA1-knockdown abolished planarian regeneration and homeostasis, compromised stem cell maintenance and PIWI-interacting RNA (piRNA) biogenesis, and deregulated SMEDWI-1/2 target genes. Mechanistically, we observed that DNAJA1 is required for the stability of SMEDWI-1 and SMEDWI-2 proteins. Furthermore, we noted that human DNAJA1 binds to Piwi-like RNA-mediated gene silencing 1 (PIWIL1) and is required for PIWIL1 stability in human gastric cancer cells. In summary, our results reveal not only an evolutionarily conserved functional link between PIWI and DNAJA1 that is essential for PIWI protein stability and piRNA biogenesis, but also an important role of DNAJA1 in the control of proteins involved in stem cell regulation.
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Pammer, Johannes, Heidi Rossiter, Martin Bilban, Leopold Eckhart, Maria Buchberger, Laura Monschein, and Michael Mildner. "PIWIL-2 and piRNAs are regularly expressed in epithelia of the skin and their expression is related to differentiation." Archives of Dermatological Research 312, no. 10 (March 12, 2020): 705–14. http://dx.doi.org/10.1007/s00403-020-02052-7.

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Abstract PIWI proteins play multiple roles in germline stem cell maintenance and self-renewal. PIWI-interacting RNAs (piRNAs) associate with PIWI proteins, form effector complexes and maintain genome integrity and function in the regulation of gene expression by epigenetic modifications. Both are involved in cancer development. In this study, we investigated the expression of PIWIL-2 and piRNAs in normal human skin and epithelial tumors and its regulation during keratinocyte (KC) differentiation. Immunohistochemistry showed that PIWIL-2 was regularly expressed in the epidermis and adnexal tissue with strongest expression in sebaceous glands. Cell culture studies revealed an association of PIWIL-2 expression with the state of differentiated KC. In contrast, the PIWIL-2 expression pattern did not correlate with stem cell compartments or malignancy. piRNAs were consistently detected in KC in vitro by next-generation sequencing and the expression levels of numerous piRNAs were regulated during KC differentiation. Epidermal piRNAs were predominantly derived from processed snoRNAs (C/D-box snoRNAs), tRNAs and protein coding genes. Our data indicate that components of the PIWIL-2—piRNA pathway are present in epithelial cells of the skin and are regulated in the context of KC differentiation, suggesting a role of somatic gene regulation. However, putative roles in the maintenance of stem cell compartments or the development of malignancy in the skin were not supported by this study.
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Ishino, Kyoko, Hidetoshi Hasuwa, Jun Yoshimura, Yuka W. Iwasaki, Hidenori Nishihara, Naomi M. Seki, Takamasa Hirano, et al. "Hamster PIWI proteins bind to piRNAs with stage-specific size variations during oocyte maturation." Nucleic Acids Research 49, no. 5 (February 15, 2021): 2700–2720. http://dx.doi.org/10.1093/nar/gkab059.

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Abstract In animal gonads, transposable elements are actively repressed to preserve genome integrity through the PIWI-interacting RNA (piRNA) pathway. In mice, piRNAs are abundantly expressed in male germ cells, and form effector complexes with three distinct PIWIs. The depletion of individual Piwi genes causes male-specific sterility with no discernible phenotype in female mice. Unlike mice, most other mammals have four PIWI genes, some of which are expressed in the ovary. Here, purification of PIWI complexes from oocytes of the golden hamster revealed that the size of the PIWIL1-associated piRNAs changed during oocyte maturation. In contrast, PIWIL3, an ovary-specific PIWI in most mammals, associates with short piRNAs only in metaphase II oocytes, which coincides with intense phosphorylation of the protein. An improved high-quality genome assembly and annotation revealed that PIWIL1- and PIWIL3-associated piRNAs appear to share the 5′-ends of common piRNA precursors and are mostly derived from unannotated sequences with a diminished contribution from TE-derived sequences, most of which correspond to endogenous retroviruses. Our findings show the complex and dynamic nature of biogenesis of piRNAs in hamster oocytes, and together with the new genome sequence generated, serve as the foundation for developing useful models to study the piRNA pathway in mammalian oocytes.
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Ross, Robert J., Molly M. Weiner, and Haifan Lin. "PIWI proteins and PIWI-interacting RNAs in the soma." Nature 505, no. 7483 (January 2014): 353–59. http://dx.doi.org/10.1038/nature12987.

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Han, Yi-Neng, Yuan Li, Sheng-Qiang Xia, Yuan-Yuan Zhang, Jun-Hua Zheng, and Wei Li. "PIWI Proteins and PIWI-Interacting RNA: Emerging Roles in Cancer." Cellular Physiology and Biochemistry 44, no. 1 (2017): 1–20. http://dx.doi.org/10.1159/000484541.

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P-Element induced wimpy testis (PIWI)-interacting RNAs (piRNAs) are a type of noncoding RNAs (ncRNAs) and interact with PIWI proteins. piRNAs were primarily described in the germline, but emerging evidence revealed that piRNAs are expressed in a tissue-specific manner among multiple human somatic tissue types as well and play important roles in transposon silencing, epigenetic regulation, gene and protein regulation, genome rearrangement, spermatogenesis and germ stem-cell maintenance. PIWI proteins were first discovered in Drosophila and they play roles in spermatogenesis, germline stem-cell maintenance, self-renewal, retrotransposons silencing and the male germline mobility control. A growing number of studies have demonstrated that several piRNA and PIWI proteins are aberrantly expressed in various kinds of cancers and may probably serve as a novel biomarker and therapeutic target for cancer treatment. Nevertheless, their specific mechanisms and functions need further investigation. In this review, we discuss about the biogenesis, functions and the emerging role of piRNAs and PIWI proteins in cancer, providing novel insights into the possible applications of piRNAs and PIWI proteins in cancer diagnosis and clinical treatment.
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Zhang, Heng, Ke Liu, Natsuko Izumi, Haiming Huang, Deqiang Ding, Zuyao Ni, Sachdev S. Sidhu, Chen Chen, Yukihide Tomari, and Jinrong Min. "Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2." Proceedings of the National Academy of Sciences 114, no. 47 (November 8, 2017): 12483–88. http://dx.doi.org/10.1073/pnas.1711486114.

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The P-element–induced wimpy testis (PIWI)-interacting RNA (piRNA) pathway plays a central role in transposon silencing and genome protection in the animal germline. A family of Tudor domain proteins regulates the piRNA pathway through direct Tudor domain–PIWI interactions. Tudor domains are known to fulfill this function by binding to methylated PIWI proteins in an arginine methylation-dependent manner. Here, we report a mechanism of methylation-independent Tudor domain–PIWI interaction. Unlike most other Tudor domains, the extended Tudor domain of mammalian Tudor domain-containing protein 2 (TDRD2) preferentially recognizes an unmethylated arginine-rich sequence from PIWI-like protein 1 (PIWIL1). Structural studies reveal an unexpected Tudor domain-binding mode for the PIWIL1 sequence in which the interface of Tudor and staphylococcal nuclease domains is primarily responsible for PIWIL1 peptide recognition. Mutations disrupting the TDRD2–PIWIL1 interaction compromise piRNA maturation via 3′-end trimming in vitro. Our work presented here reveals the molecular divergence of the interactions between different Tudor domain proteins and PIWI proteins.
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Arkov, Alexey L. "RNA Selection by PIWI Proteins." Trends in Biochemical Sciences 43, no. 3 (March 2018): 153–56. http://dx.doi.org/10.1016/j.tibs.2017.12.007.

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Shi, Shuo, Zhen-Zhen Yang, Sanhong Liu, Fan Yang, and Haifan Lin. "PIWIL1 promotes gastric cancer via a piRNA-independent mechanism." Proceedings of the National Academy of Sciences 117, no. 36 (August 26, 2020): 22390–401. http://dx.doi.org/10.1073/pnas.2008724117.

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Targeted cancer therapy aims to achieve specific elimination of cancerous but not normal cells. Recently, PIWI proteins, a subfamily of the PAZ-PIWI domain (PPD) protein family, have emerged as promising candidates for targeted cancer therapy. PPD proteins are essential for small noncoding RNA pathways. The Argonaute subfamily partners with microRNA and small interfering RNA, whereas the PIWI subfamily partners with PIWI-interacting RNA (piRNA). Both PIWI proteins and piRNA are mostly expressed in the germline and best known for their function in transposon silencing, with no detectable function in mammalian somatic tissues. However, PIWI proteins become aberrantly expressed in multiple types of somatic cancers, thus gaining interest in targeted therapy. Despite this, little is known about the regulatory mechanism of PIWI proteins in cancer. Here we report that one of the four PIWI proteins in humans, PIWIL1, is highly expressed in gastric cancer tissues and cell lines. Knocking out the PIWIL1 gene (PIWIL1-KO) drastically reduces gastric cancer cell proliferation, migration, metastasis, and tumorigenesis. RNA deep sequencing of gastric cancer cell line SNU-1 reveals that KO significantly changes the transcriptome, causing the up-regulation of most of its associated transcripts. Surprisingly, few bona fide piRNAs exist in gastric cancer cells. Furthermore, abolishing the piRNA-binding activity of PIWIL1 does not affect its oncogenic function. Thus, PIWIL1 function in gastric cancer cells is independent of piRNA. This piRNA-independent regulation involves interaction with the UPF1-mediated nonsense-mediated mRNA decay (NMD) mechanism. Altogether, our findings reveal a piRNA-independent function of PIWIL1 in promoting gastric cancer.
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Betting, Valerie, Joep Joosten, Rebecca Halbach, Melissa Thaler, Pascal Miesen, and Ronald P. Van Rij. "A piRNA-lncRNA regulatory network initiates responder and trailer piRNA formation during mosquito embryonic development." RNA 27, no. 10 (July 1, 2021): 1155–72. http://dx.doi.org/10.1261/rna.078876.121.

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PIWI-interacting (pi)RNAs are small silencing RNAs that are crucial for the defense against transposable elements in germline tissues of animals. In Aedes aegypti mosquitoes, the piRNA pathway also contributes to gene regulation in somatic tissues, illustrating additional roles for piRNAs and PIWI proteins besides transposon repression. Here, we identify a highly abundant endogenous piRNA (propiR1) that associates with both Piwi4 and Piwi5. PropiR1-mediated target silencing requires base-pairing in the seed region with supplemental base-pairing at the piRNA 3′ end. Yet, propiR1 represses a limited set of targets, among which is the lncRNA AAEL027353 (lnc027353). Slicing of lnc027353 initiates production of responder and trailer piRNAs from the cleavage fragment. Expression of propiR1 commences early during embryonic development and mediates degradation of maternally provided lnc027353. Both propiR1 and its lncRNA target are conserved in the closely related Aedes albopictus mosquito, underscoring the importance of this regulatory network for mosquito development.
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Dissertations / Theses on the topic "Piwi proteins"

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Bagijn, Marloes Pauline. "Genetic and functional characterization of the Piwi proteins and piRNAs of Caenorhabditis elegans." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609250.

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Kim, Iana [Verfasser], and Claus-Dieter [Akademischer Betreuer] Kuhn. "On piRNAs and PIWI proteins in Schmidtea mediterranea and their role in mRNA surveillance of adult stem cells / Iana Kim ; Betreuer: Claus-Dieter Kuhn." Bayreuth : Universität Bayreuth, 2020. http://d-nb.info/1210999617/34.

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Eckhardt, Stephanie. "Le complexe MILI/mHEN1 et études fonctionnelles des protéines DrTDRD1 et DrMOV10L." Phd thesis, Université de Grenoble, 2011. http://tel.archives-ouvertes.fr/tel-00601225.

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Les protéines Argonaute sont associées à de petits ARN et participent à la régulation de l'expression des gènes. Les protéines Piwi, sous-famille des protéines Argonaute, sont principalement exprimées dans les lignées germinales. Elles recrutent les piRNA (Piwi-interacting RNA) et assurent la stabilité du génome en inhibant les transposons. Une caractéristique des piRNA est la présence de groupes 2'-O-methyl à l'extrémité 3'. Les microARN et siRNA (small interfering RNA) de plantes, comme les siRNA de Drosophyle portent aussi cette modification qui est catalysée par l'ARN méthyl-tranférase HEN1. Son homologue murin, mHEN1, méthyle in vitro de petits ARN, mais son rôle dans la voie des piRNA n'avait pas encore été envisagé. Mon objectif était de relier mHEN1 à la voie des piRNA. J'ai démontré que mHEN1 interagit directement avec la partie N-ter de MILI mais pas avec les autres protéines Piwi de souris. La partie N-ter de MILI porte des arginines méthylées. J'ai démontré que l'interaction ne dépendait pas de la présence de cette modification, ce qui suggère que mHEN1 intervient avant la modification de MILI. Par imagerie cellulaire j'ai montré la compartimentation de HEN1 et des protéines Piwi dans des granules cytoplasmiques différents. Parallèlement, afin de caractériser les éléments de la voie piRNA, j'ai développé un nouveau modèle d'étude basé sur des embryons de poisson zèbre (Danio rerio). Ainsi, j'ai évalué le rôle de deux protéines interagissant avec les protéines Piwi, TDRD1 (Tudor-domain containing) et l'hélicase MOV10l décrits chez la souris mais pas chez le poisson zèbre. J'ai montré que l'expression de DrTDRD1, spécifique à la lignée germinale, dépend de sa partie 3'UTR. La réduction de l'expression de DrMOV10l, obtenue grâce à l'utilisation de morpholinos, entraîne la dérépression des éléments rétrotransposables des embryons en développement. Cette technique de Knock Down sera utilisée pour identifier de nouveaux éléments de la biogenèse des piRNA.
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Merrifield, Matthew, and University of Lethbridge Faculty of Arts and Science. "Radiation-induced deregulation of PiRNA pathway proteins : a possible molecular mechanism underlying transgenerational epigenomic instability." Thesis, Lethbridge, Alta. : University of Lethbridge, Dept. of Biological Science, c2011, 2011. http://hdl.handle.net/10133/2617.

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PiRNAs and their Piwi family protein partners are part of a germline specific epigenetic regulatory mechanism essential for proper spermatogenesis, silencing of transposable elements, and maintaining germline genome integrity, yet their role in the response of the male germline to genotoxic stress is unknown. Ionizing radiation (IR) is known to cause transgenerational genome instability that is linked to carcinogenesis. Although the molecular etiology of IR-induced transgenerational genomic instability is not fully understood, it is believed to be an epigenetically mediated phenomenon. IR-induced alterations in the expression pattern of key regulatory proteins involved in the piRNA pathway essential for paternal germline genome stability may be directly involved in producing epigenetic alterations that can impact future generations. Here we show whole body and localized X-irradiation leads to significant altered expression of proteins that are necessary for, and intimately involved in, the proper functioning of the germline specific piRNA pathway in mice and rats. In addition we found that IR-induced alterations to piRNA pathway protein levels were time and dose dependent.
ix, 123 leaves : ill. (some col.) ; 29 cm
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Vargas, Aguilar Stephanie. "A novel mammalian PIWI protein regulates self-renewal and lifespan of macrophages." Doctoral thesis, Humboldt-Universität zu Berlin, 2019. http://dx.doi.org/10.18452/20073.

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PIWI Proteine sind die zentralen Darsteller eines RNA-basierten Mechanismus, der die Mobilisierung transponierbarer Elemente im Genom unterdrückt, um genetische Stabilität zu gewährleisten. Demzufolge sind PIWI-Proteine für die langfristige Erhaltung verschiedener Stamzellpopulationen notwendig. Beispiele dafür sind verschiedene adulte somatische Stammzellen in Drosophila und die Stammzellen der Keimbahn aller bisher untersuchten Tierarten. Bei Säugetieren sind die beschriebenen Funktionen von PIWI Proteinen strikt auf die männliche Keimbahn beschränkt. Trotz Andeutungen auf eine Rolle von PIWI-Proteinen in somatischen Zellen von Säugetieren, wurde eine Funktion bisher nicht beschrieben. Ähnlich wie Stammzellen, können sich Makrophagen in verschiedenen Geweben selbst-erneuern, um ihre Populationen zu erhalten. Diese Selbsterneuerung beruht auf der geringen Expression der Transkriptionsfaktoren MafB und cMaf, was die Aktivierung eines stammzell-ähnliches Gen-Netzwerk, das die Proliferation vorantreibt. Makrophagen mit einer genetischen Deletion von MafB und cMaf (MafDKO-Makrophagen) oder Makrophagen mit natürlich niedriger Expression von MafB oder cMaf, wie z.B. alveoläre Makrophagen, weisen dementsprechend eine erweiterte Kapazität zur Selbsterneuerung auf. Wie haben festgestellt, dass eine kurze Isoform des Maus- Gens Piwil2, die wir ‚Piwito’ genannt haben, in MafDKO und alveolären Makrophagen exprimiert wird. Die Expression von Piwito ist für die normale Selbsterneuerung der untersuchten Makrophagen notwendig, wie die in vitro und in vivo Untersuchungen darlegen. Eine Abwesenheit von Piwito in alveolären Makrophagen führt zu einer Verkürzung derer Lebenspanne in Kultur. Außerdem beweisen wir, dass Piwito von MafB in nicht-proliferierenden Makrophagen gebunden und unterdrückt wird. Diese Studie ist somit der erste Bericht über eine somatische Funktion von PIWI-Proteinen in nicht transformierten Zellen von Säugetieren.
PIWI proteins are the main players of an RNA-based gene regulatory machinery that represses transposable elements in the genome to prevent their mobilization and ensure genetic stability. PIWI proteins have thus highly conserved stem-cell functions. They are indispensable for the long-term maintenance of the somatic stem cells that drive regeneration in invertebrates, of various adult somatic stem cells in Drosophila and, most prominently, of the germline of all species studied so far. In mammals, their described functions are strictly restricted to the male germline. Despite suggestive observations for a role of PIWI proteins in the mammalian soma, robust evidence remains absent. Similar to stem cells, tissue macrophages can locally self-renew to maintain their populations. Mechanistically, their self-renewal relies on low expression of the macrophage transcription factors MafB and cMaf, since it allows the induction of a stem cell-like network of genes that drives proliferation. Macrophages with a genetic deletion of MafB and cMaf (MafDKO macrophages) acquire therefore the capacity to self-renew, defined by an indefinite growth in culture that does not comprise their identity and does not involve cancerogenic transformation. Similarly, macrophages with naturally low levels of MafB or cMaf, such as alveolar macrophages, display an extended self-renewal capacity in vivo and in vitro. We have found that a short isoform of the murine Piwil2 gene, that we named ‘Piwito’, is expressed in MafDKO and alveolar macrophages. Piwito expression is necessary for the unaltered self-renewal of macrophages, as shown by in vitro and in vivo assays. To highlight is the fact that Piwito deficiency limits the extended lifespan of alveolar macrophages in culture. Additionally, we show that Piwito is bound and repressed by MafB in quiescent macrophages. This study thus represents the first report of a somatic function for mammalian PIWI proteins in non-transformed cells.
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Balaratnam, Sumirtha. "BIOGENESIS AND FUNCTIONAL APPLICATIONS OF PIWI INTERACTING RNAs (piRNAs)." Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1531753741509242.

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Berry, Jamie. "Structural characterization of type IV pilus biogenesis proteins." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/structural-characterization-of-type-iv-pilus-biogenesis-proteins(1e0d7119-58d5-4e5d-839d-daef8deb76ab).html.

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Type IV pili, or fimbriae, are long, thin proteinaceous appendages found on the surface of many well-known pathogens. They mediate a variety of important virulence functions for the organism, such as twitching motility, biofilm formation, uptake of genetic material and host cell recognition and adhesion. Pili are formed by the rapid polymerization and de-polymerization of the pilin subunit, and this is orchestrated by a complex macromolecular machine which spans the bacterial cell envelope, requiring a variety of gene products. The type IV pilus biogenesis system is closely related to the bacterial type II secretion system, one of six designated multi-protein cell envelope complexes which are dedicated to the specific secretion of exotoxins and virulence factors. Many of these secretion systems also produce fimbrial structures to facilitate the extrusion of their substrates or to communicate with the host. As they form crucial virulence factors, the secretion systems and the type IV pilus biogenesis system have become attractive potential antimicrobial targets and obtaining structural and functional information for the components of these systems is an important first step towards achieving this.Type IV pili appear on the surface of bacteria through an outer membrane pore, PilQ, which is a member of the secretin family. Secretins are also found in the type II and III secretion systems, but the way in which they are regulated remains unclear. PilQ forms a dodecameric chamber in the outer membrane with a large vestibule which reaches into the periplasm, composed of its N-terminal domains. In this project, N-terminal domains from PilQ were produced in recombinant form and their structures determined by NMR. One of these domains revealed an eight-stranded beta-sandwich structure which appears to be unique to type IV pilus secretins and has not been structurally characterized before. Another revealed an alpha/beta type fold which is common to secretins of other systems. In the second part of this project, the interaction formed between the N-terminal alpha/beta domains of PilQ and an essential inner membrane-anchored lipoprotein, PilP, was probed by NMR chemical shift perturbation. Based on changes to the 15N-HSQC spectra the binding site was mapped onto each protein to produce a computational model for the complex formed between the two. Using a recent cryo-EM structure for the Neisseria PilQ dodecamer determined by colleagues, it was possible to model the PilQ N-terminal domains in complex with PilP into the electron density map. This produced a model for the trans-periplasmic assembly formed by PilQ and PilP in the type IV pilus biogenesis system, and led to the conclusion that the PilQ dodecamer needs to disassemble considerably at the base to accommodate a pilus fibre. The novel beta-domains might therefore function to gate or open the secretin, and PilP may play a role in stabilizing the secretin during this and serve to connect the outer and inner membrane system components.
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Mösinger, Carina [Verfasser], Hermann M. [Akademischer Betreuer] Behre, Jürgen [Akademischer Betreuer] Dittmer, and Holger [Akademischer Betreuer] Herlyn. "Die Rolle der Proteine Piwi-like 1 und Piwi-like 3 für die Spermatogenese des Menschen und die männliche Fertilität / Carina Mösinger ; Hermann M. Behre, Jürgen Dittmer, Holger Herlyn." Halle, 2016. http://d-nb.info/1117028240/34.

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Selim, Khaled [Verfasser]. "Structural and Functional Characterization of PII and PII-like Proteins and their Network of Interactions / Khaled Selim." Tübingen : Universitätsbibliothek Tübingen, 2021. http://d-nb.info/1233678507/34.

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Shirdel, Mariam. "Probing protein - Pili interactions by optical tweezers and 3D molecular modelling." Thesis, Umeå universitet, Institutionen för fysik, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-68747.

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Books on the topic "Piwi proteins"

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Holmgren, Anders. Structural studies of PapD, a chaperone protein involved in pili assembly, from E. coli. Uppsala: Sveriges Lantbruksuniversitet, 1993.

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Testut, Jean-Francois. Evidence for the occurence of a pea chlorplast protein in haustoria of the powdery mildew fungus,erysiphe pisi. Birmingham: University of Birmingham, 1997.

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Leckie, Malcolm Peter. In situ imaging and protein analysis of host subcellular structures during the infection of pea by Erysiphe pisi. Birmingham: University of Birmingham, 1996.

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Kirchman, David L. Elements, biochemicals, and structures of microbes. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198789406.003.0002.

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Microbiologists focus on the basic biochemical make-up of microbes, such as relative amounts of protein, RNA, and DNA in cells, while ecologists and biogeochemists use elemental ratios, most notably, the ratio of carbon to nitrogen (C:N), to explore biogeochemical processes and to connect up the carbon cycle with the cycle of other elements. Microbial ecologists make use of both types of data and approaches. This chapter combines both and reviews all things, from elements to macromolecular structures, that make up bacteria and other microbes. The most commonly used elemental ratio was discovered by Alfred Redfield who concluded that microbes have a huge impact on the chemistry of the oceans because of the similarity in nitrogen-to-phosphorus ratios for organisms and nitrate-to-phosphate ratios in the deep oceans. Although statistically different, the C:N ratios in soil microbes are remarkably similar to the ratios of aquatic microbes. The chapter moves on to discussing the macromolecular composition of bacteria and other microbes. This composition gives insights into the growth state of microbes in nature. Geochemists use specific compounds, “biomarkers”, to trace sources of organic material in ecosystems. The last section of the chapter is a review of extracellular polymers, pili, and flagella, which serve a variety of functions, from propelling microbes around to keeping them stuck in one place.
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Book chapters on the topic "Piwi proteins"

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Honda, Shozo, Yoriko Kirino, and Yohei Kirino. "Analysis of sDMA Modifications of PIWI Proteins." In Methods in Molecular Biology, 137–48. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-694-8_11.

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Vourekas, Anastassios, and Zissimos Mourelatos. "HITS-CLIP (CLIP-Seq) for Mouse Piwi Proteins." In Methods in Molecular Biology, 73–95. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-694-8_7.

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Clark, Josef P., and Nelson C. Lau. "Piwi Proteins and piRNAs Step onto the Systems Biology Stage." In Systems Biology of RNA Binding Proteins, 159–97. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1221-6_5.

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Muschiol, Sandra, Marie-Stephanie Aschtgen, Priyanka Nannapaneni, and Birgitta Henriques-Normark. "Gram-Positive Type IV Pili and Competence." In Protein Secretion in Bacteria, 129–35. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch11.

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Barckmann, Bridlin, Jérémy Dufourt, and Martine Simonelig. "iCLIP of the PIWI Protein Aubergine in Drosophila Embryos." In mRNA Decay, 89–110. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7540-2_7.

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Psonis, John J., and David G. Thanassi. "Therapeutic Approaches Targeting the Assembly and Function of Chaperone-Usher Pili." In Protein Secretion in Bacteria, 149–61. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch13.

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Benelli, E. M., E. M. Souza, M. G. Yates, L. U. Rigo, M. Buck, M. Moore, A. Harper, and F. O. Pedrosa. "The PII Protein of Herbaspirillum Seropedicae." In Highlights of Nitrogen Fixation Research, 201–5. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4795-2_40.

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Contreras, Fernanda, and Jaime Andrés Rivas-Pardo. "Interfering with the Folding of Group A Streptococcal pili Proteins." In Methods in Molecular Biology, 347–64. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0467-0_28.

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Reuter, Michael, and Ramesh S. Pillai. "Analysis of Small RNA-Guided Endonuclease Activity in Endogenous Piwi Protein Complexes from Mouse Testes." In Methods in Molecular Biology, 111–21. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-694-8_9.

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Forchhammer, Karl. "The Network of PII Signalling Protein Interactions in Unicellular Cyanobacteria." In Recent Advances in Phototrophic Prokaryotes, 71–90. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-1528-3_5.

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Conference papers on the topic "Piwi proteins"

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Moisés, Jorge, Alfons Navarro, Rut Tejero, Nuria Viñolas, Anna Cordeiro, Ramón M. Marrades, Dolors Fuster, et al. "PIWI proteins as prognostic markers in non small cell lung cancer." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa4238.

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Lee, Jing Yi, Wai Cheong Yip, and Qidong Hu. "Abstract A29: PIWI-like proteins and piRNAs in breast cancer cell proliferation and migration." In Abstracts: AACR Special Conference: Chromatin and Epigenetics in Cancer; September 24-27, 2015; Atlanta, GA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.chromepi15-a29.

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Eckstein, Markus, Rudolf Jung, Katrin Weigelt, Danijel Sikic, Robert Stöhr, Carol Geppert, Abbas Agaimy, et al. "Abstract 3674: Protein levels of Piwi-like 1 and -2 protein are prognostic factors for muscle invasive urothelial bladder cancer patients." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3674.

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Eckstein, Markus, Rudolf Jung, Katrin Weigelt, Danijel Sikic, Robert Stöhr, Carol Geppert, Abbas Agaimy, et al. "Abstract 3674: Protein levels of Piwi-like 1 and -2 protein are prognostic factors for muscle invasive urothelial bladder cancer patients." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3674.

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Ilmiya, Istifadatul, Hening Ryan Aryani, Nur Rohmah Prihatanti, Dwi Yuni Nur Hidayati, and Noorhamdani Noorhamdani. "Identification of hemagglutinin protein from Streptococcus agalactiae pili in mice erythrocytes as a vaccine candidate." In INTERNATIONAL CONFERENCE ON LIFE SCIENCES AND TECHNOLOGY (ICoLiST 2020). AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0052701.

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