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Journal articles on the topic 'Ribonucleoprotein particles RNPs'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Peek, R., G. J. Pruijn, A. J. van der Kemp, and W. J. van Venrooij. "Subcellular distribution of Ro ribonucleoprotein complexes and their constituents." Journal of Cell Science 106, no. 3 (1993): 929–35. http://dx.doi.org/10.1242/jcs.106.3.929.

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Ro ribonucleoprotein particles (Ro RNPs) are complexes of several proteins with a small RNA polymerase III-transcribed Ro RNA. Despite their relative abundance and evolutionary conservation no function has as yet been ascribed to these complexes. Also their subcellular distribution is still largely unknown as immunofluorescence studies concerning their localization have produced conflicting data. We have used cell enucleation to fractionate cells into cytoplasmic and nuclear fractions. Analysis of these fractions revealed an exclusively cytoplasmic localization for the Ro RNPs. The majority of

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2

Liang, Bo, and Hong Li. "Structures of ribonucleoprotein particle modification enzymes." Quarterly Reviews of Biophysics 44, no. 1 (2010): 95–122. http://dx.doi.org/10.1017/s0033583510000235.

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AbstractSmall nucleolar and Cajal body ribonucleoprotein particles (RNPs) are required for the maturation of ribosomes and spliceosomes. They consist of small nucleolar RNA or Cajal body RNA combined with partner proteins and represent the most complex RNA modification enzymes. Recent advances in structure and function studies have revealed detailed information regarding ribonucleoprotein assembly and substrate binding. These enzymes form intertwined RNA–protein assemblies that facilitate reversible binding of the large ribosomal RNA or small nuclear RNA. These revelations explain the specific

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3

Simons, F. H., G. J. Pruijn, and W. J. van Venrooij. "Analysis of the intracellular localization and assembly of Ro ribonucleoprotein particles by microinjection into Xenopus laevis oocytes." Journal of Cell Biology 125, no. 5 (1994): 981–88. http://dx.doi.org/10.1083/jcb.125.5.981.

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Xenopus laevis oocytes have been used to determine the intracellular localization of components of Ro ribonucleoprotein particles (Ro RNPs) and to study the assembly of these RNA-protein complexes. Microinjection of the protein components of human Ro RNPs, i.e., La, Ro60, and Ro52, in X. laevis oocytes showed that all three proteins are able to enter the nucleus, albeit with different efficiencies. In contrast, the RNA components of human Ro RNPs (the Y RNAs) accumulate in the X. laevis cytoplasm upon injection. Localization studies performed at low temperatures indicated that both nuclear imp

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4

Peek, R., G. J. Pruijn, and W. J. van Venrooij. "Epitope specificity determines the ability of anti-Ro52 autoantibodies to precipitate Ro ribonucleoprotein particles." Journal of Immunology 153, no. 9 (1994): 4321–29. http://dx.doi.org/10.4049/jimmunol.153.9.4321.

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Abstract Ro ribonucleoprotein particles (Ro RNPs) are evolutionarily conserved cytoplasmic complexes of unknown function. They are composed of several proteins and a small, RNA polymerase III-transcribed Ro or Y RNA. Abs directed against the protein moiety of Ro RNPs are often found in sera of patients suffering from certain autoimmune disorders. The association of one of the Ro proteins, a protein of 52 kDa (Ro52), with Ro RNPs is still questionable. In this study, we have used anti-Ro52 Abs isolated from autoimmune sera to locate the antigenic determinants of Ro52 and to analyze the correlat

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5

Hall, Kathleen B. "RNA and Proteins: Mutual Respect." F1000Research 6 (March 27, 2017): 345. http://dx.doi.org/10.12688/f1000research.10572.1.

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Proteins and RNA are often found in ribonucleoprotein particles (RNPs), where they function in cellular processes to synthesize proteins (the ribosome), chemically modify RNAs (small nucleolar RNPs), splice pre-mRNAs (the spliceosome), and, on a larger scale, sequester RNAs, degrade them, or process them (P bodies, Cajal bodies, and nucleoli). Each RNA–protein interaction is a story in itself, as both molecules can change conformation, compete for binding sites, and regulate cellular functions. Recent studies of Xist long non-coding RNP, the U4/5/6 tri-small nuclear RNP complex, and an activat

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6

Bachmann, M., W. J. Mayet, H. C. Schröder, K. Pfeifer, K. H. Meyer zum Büschenfelde, and W. E. G. Müller. "Identification of the Ro and La antigens in the endoribonuclease VII–ribonucleoprotein complex." Biochemical Journal 243, no. 1 (1987): 189–94. http://dx.doi.org/10.1042/bj2430189.

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45 S RNP (ribonucleoprotein) particles from calf thymus or L5178y mouse lymphoma cells contain the poly(A)-modulated and oligo(U)-binding endoribonuclease VII [Bachmann, Zahn & Müller (1983) J. Biol. Chem. 258, 7033-7040]. From these particles a 4.5 S RNA was isolated that possesses an oligo(U) sequence. By using monospecific and non-cross-reacting antibodies directed against the La or Ro antigen, both proteins were identified in the endoribonuclease VII-RNP complex after phosphorylation in vitro. In a second approach, endoribonuclease VII activity was identified in immunoaffinity-purified

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7

Wurtz-T, E. Kiseleva, G. Nacheva, A. Alzhanova-Ericcson, A. Rosén, and B. Daneholt. "Identification of two RNA-binding proteins in Balbiani ring premessenger ribonucleoprotein granules and presence of these proteins in specific subsets of heterogeneous nuclear ribonucleoprotein particles." Molecular and Cellular Biology 16, no. 4 (1996): 1425–35. http://dx.doi.org/10.1128/mcb.16.4.1425.

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Balbiani ring (BR) granules are premessenger ribonucleoprotein particles (RNPs) generated in giant chromosomal puffs, the BRs, in the larval salivary glands of the dipteran chironomus tentans. Monoclonal antibodies were raised against nuclear proteins collected on a single-stranded-DNA-agarose affinity column, and two of them were used to identify RNA-binding proteins in BR granules. First, in Western blots (immunoblots), one of the antibodies recognized a 36-kDa protein and the other recognized a 45-KDa protein. Second, both antibodies bound to the BRs in immunocytological experiments. It was

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8

Kedersha, Nancy L., and Leonard H. Rome. "Immunolocalization of vault particles in cultured cells." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (1992): 458–59. http://dx.doi.org/10.1017/s0424820100122691.

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We first reported on the existence of vault ribonucleoprotein particles in 1986, and since this study we have demonstrated that these unusual RNPs are ubiquitously expressed and highly conserved among diverse eukaryotes. These particles are quite large (65 x 35 nm) and distinctly regular in shape and dimensions. The polypeptide composition of vaults is also similar between species, dominated by a∼100 Kd protein which makes up >70% of the particles mass. The RNA component of vaults, which has been sequenced and characterized from both rat and bullfrog, does not appear to serve a structural r

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9

Zillmann, M., M. L. Zapp, and S. M. Berget. "Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles." Molecular and Cellular Biology 8, no. 2 (1988): 814–21. http://dx.doi.org/10.1128/mcb.8.2.814-821.1988.

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Assembly of splicing precursor RNAs into ribonucleoprotein particle (RNP) complexes during incubation in in vitro splicing extracts was monitored by a new system of RNP gel electrophoresis. The temporal pattern of assembly observed by our system was identical to that obtained by other gel and gradient methodologies. In contrast to the results obtained by other systems, however, we observed requirements of U1 small nuclear RNPs (snRNPs) and 5' splice junction sequences for formation of specific complexes and retention of U1 snRNPs within gel-fractionated complexes. Single-intron substrate RNAs

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10

Zillmann, M., M. L. Zapp, and S. M. Berget. "Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles." Molecular and Cellular Biology 8, no. 2 (1988): 814–21. http://dx.doi.org/10.1128/mcb.8.2.814.

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Assembly of splicing precursor RNAs into ribonucleoprotein particle (RNP) complexes during incubation in in vitro splicing extracts was monitored by a new system of RNP gel electrophoresis. The temporal pattern of assembly observed by our system was identical to that obtained by other gel and gradient methodologies. In contrast to the results obtained by other systems, however, we observed requirements of U1 small nuclear RNPs (snRNPs) and 5' splice junction sequences for formation of specific complexes and retention of U1 snRNPs within gel-fractionated complexes. Single-intron substrate RNAs

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11

Liu, Chengyu, and L. Dennis Smith. "In vivo storage of XR family interspersed RNA in Xenopus oocytes." Zygote 3, no. 1 (1995): 37–44. http://dx.doi.org/10.1017/s0967199400002367.

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SummaryInterspersed RNA is an abundant class of cytoplasmic poly(A)+ RNA which contains repetitive elements within mostly heterogeneous single copy sequences. In spite of its quantitative importance in oocytes or eggs (two-thirds of the total poly(A)+ RNA), very little is known about its synthesis, its interaction with other molecules, and its functional significance. Here, we analysed a prevalent family of interspersed RNa (XR family) during Xenopus oogenesis. We found that XR interspersed RNA, unlike extracted interspersed RNA, did not form RNA duplexes in vivo. Im small oocytes (stage III),

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12

Patton, J. R. "Pseudouridine modification of U5 RNA in ribonucleoprotein particles assembled in vitro." Molecular and Cellular Biology 11, no. 12 (1991): 5998–6006. http://dx.doi.org/10.1128/mcb.11.12.5998-6006.1991.

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The formation of pseudouridine (psi) in U5 RNA during ribonucleoprotein (RNP) assembly was investigated by using HeLa cell extracts. In vitro transcribed, unmodified U5 RNA assembled into an RNP particle with the same buoyant density and sedimentation velocity as did U5 small nuclear RNP from extracts. The greatest amount of psi modification was detected when a combination of S100 and nuclear extracts was used for assembly. psi formation was inhibited when ATP and creatine phosphate or MgCl2 were not included in the assembly reaction, paralleling the inhibition of RNP particle formation. A tim

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Patton, J. R. "Pseudouridine modification of U5 RNA in ribonucleoprotein particles assembled in vitro." Molecular and Cellular Biology 11, no. 12 (1991): 5998–6006. http://dx.doi.org/10.1128/mcb.11.12.5998.

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The formation of pseudouridine (psi) in U5 RNA during ribonucleoprotein (RNP) assembly was investigated by using HeLa cell extracts. In vitro transcribed, unmodified U5 RNA assembled into an RNP particle with the same buoyant density and sedimentation velocity as did U5 small nuclear RNP from extracts. The greatest amount of psi modification was detected when a combination of S100 and nuclear extracts was used for assembly. psi formation was inhibited when ATP and creatine phosphate or MgCl2 were not included in the assembly reaction, paralleling the inhibition of RNP particle formation. A tim

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14

Kuhn-Holsken, E., O. Dybkov, B. Sander, R. Luhrmann, and H. Urlaub. "Improved identification of enriched peptide RNA cross-links from ribonucleoprotein particles (RNPs) by mass spectrometry." Nucleic Acids Research 35, no. 15 (2007): e95-e95. http://dx.doi.org/10.1093/nar/gkm540.

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15

García-Rodríguez, Fernando M., José L. Neira, Marco Marcia, María D. Molina-Sánchez та Nicolás Toro. "A group II intron-encoded protein interacts with the cellular replicative machinery through the β-sliding clamp". Nucleic Acids Research 47, № 14 (2019): 7605–17. http://dx.doi.org/10.1093/nar/gkz468.

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Abstract Group II introns are self-splicing mobile genetic retroelements. The spliced intron RNA and the intron-encoded protein (IEP) form ribonucleoprotein particles (RNPs) that recognize and invade specific DNA target sites. The IEP is a reverse transcriptase/maturase that may bear a C-terminal endonuclease domain enabling the RNP to cleave the target DNA strand to prime reverse transcription. However, some mobile introns, such as RmInt1, lack the En domain but nevertheless retrohome efficiently to transient single-stranded DNA target sites at a DNA replication fork. Their mobility is associ

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16

Lyu, Pin, Parisa Javidi-Parsijani, Anthony Atala, and Baisong Lu. "Delivering Cas9/sgRNA ribonucleoprotein (RNP) by lentiviral capsid-based bionanoparticles for efficient ‘hit-and-run’ genome editing." Nucleic Acids Research 47, no. 17 (2019): e99-e99. http://dx.doi.org/10.1093/nar/gkz605.

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AbstractTransient expression of the CRISPR/Cas9 machinery will not only reduce risks of mutagenesis from off-target activities, but also decrease possible immune response to Cas9 protein. Building on our recent developing of a system able to package up to 100 copies of Cas9 mRNA in each lentivirus-like particle (LVLP) via the specific interaction between aptamer and aptamer-binding proteins (ABP), here we develop a lentiviral capsid-based bionanoparticle system, which allows efficient packaging of Cas9/sgRNA ribonucleoprotein (RNP). We show that replacing the Tetraloop of sgRNA scaffold with a

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Petri, Sebastian, Matthias Grimmler, Sabine Over, Utz Fischer та Oliver J. Gruss. "Dephosphorylation of survival motor neurons (SMN) by PPM1G/PP2Cγ governs Cajal body localization and stability of the SMN complex". Journal of Cell Biology 179, № 3 (2007): 451–65. http://dx.doi.org/10.1083/jcb.200704163.

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The survival motor neuron (SMN) complex functions in maturation of uridine-rich small nuclear ribonucleoprotein (RNP) particles. SMN mediates the cytoplasmic assembly of Sm proteins onto uridine-rich small RNAs, and then participates in targeting RNPs to nuclear Cajal bodies (CBs). Recent studies have suggested that phosphorylation might control localization and function of the SMN complex. Here, we show that the nuclear phosphatase PPM1G/PP2Cγ interacts with and dephosphorylates the SMN complex. Small interfering RNA knockdown of PPM1G leads to an altered phosphorylation pattern of SMN and Ge

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Tseng, Chi-Kang. "Study of Telomere and Telomerase Dynamics." Impact 2021, no. 8 (2021): 22–24. http://dx.doi.org/10.21820/23987073.2021.8.22.

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Telomerases play a key role in maintaining the necessary level of chromosomal degradation in all cells and so they are an important target for in depth molecular, genetic, and in vivo investigations. Assistant Professor Chi-Kang Tseng, Graduate Institute of Microbiology, National Taiwan University College of Medicine (NTUCM), Taiwan, specialises in the molecular biology of ribonucleoprotein particles (RNPs), primarily telomerases and spliceosomes and collaborates with clinicians and experts in related fields to ensure his work is as relevant as possible and can potentially be directly translat

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Li, Hai-Ou, Ya-Feng Zhu, Makoto Asakawa, et al. "A Cytoplasmic RNA Vector Derived from Nontransmissible Sendai Virus with Efficient Gene Transfer and Expression." Journal of Virology 74, no. 14 (2000): 6564–69. http://dx.doi.org/10.1128/jvi.74.14.6564-6569.2000.

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ABSTRACT We have recovered a virion from defective cDNA of Sendai virus (SeV) that is capable of self-replication but incapable of transmissible-virion production. This virion delivers and expresses foreign genes in infected cells, and this is the first report of a gene expression vector derived from a defective viral genome of theParamyxoviridae. First, functional ribonucleoprotein complexes (RNPs) were recovered from SeV cloned cDNA defective in the F (envelope fusion protein) gene, in the presence of plasmids expressing nucleocapsid protein and viral RNA polymerase. Then the RNPs were trans

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Patel, Snehal Bhikhu, Natalya Novikova, and Michel Bellini. "Splicing-independent recruitment of spliceosomal small nuclear RNPs to nascent RNA polymerase II transcripts." Journal of Cell Biology 178, no. 6 (2007): 937–49. http://dx.doi.org/10.1083/jcb.200706134.

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In amphibian oocytes, most lateral loops of the lampbrush chromosomes correspond to active transcriptional sites for RNA polymerase II. We show that newly assembled small nuclear ribonucleoprotein (RNP [snRNP]) particles, which are formed upon cytoplasmic injection of fluorescently labeled spliceosomal small nuclear RNAs (snRNAs), target the nascent transcripts of the chromosomal loops. With this new targeting assay, we demonstrate that nonfunctional forms of U1 and U2 snRNAs still associate with the active transcriptional units. In particular, we find that their association with nascent RNP f

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Severt, W. L., T. U. Biber, X. Wu, N. B. Hecht, R. J. DeLorenzo, and E. R. Jakoi. "The suppression of testis-brain RNA binding protein and kinesin heavy chain disrupts mRNA sorting in dendrites." Journal of Cell Science 112, no. 21 (1999): 3691–702. http://dx.doi.org/10.1242/jcs.112.21.3691.

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Ribonucleoprotein particles (RNPs) are thought to be key players in somato-dendritic sorting of mRNAs in CNS neurons and are implicated in activity-directed neuronal remodeling. Here, we use reporter constructs and gel mobility shift assays to show that the testis brain RNA-binding protein (TB-RBP) associates with mRNPs in a sequence (Y element) dependent manner. Using antisense oligonucleotides (anti-ODN), we demonstrate that blocking the TB-RBP Y element binding site disrupts and mis-localizes mRNPs containing (alpha)-calmodulin dependent kinase II (alpha)-CAMKII) and ligatin mRNAs. In addit

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Borovikova, Sofiia E., Mikhail V. Shepelev, Dmitriy V. Mazurov, and Natalia A. Kruglova. "Efficient Genome Editing Using ‘NanoMEDIC’ AsCas12a-VLPs Produced with Pol II-Transcribed crRNA." International Journal of Molecular Sciences 25, no. 23 (2024): 12768. http://dx.doi.org/10.3390/ijms252312768.

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Virus-like particles (VLPs) are an attractive vehicle for the delivery of Cas nuclease and guide RNA ribonucleoprotein complexes (RNPs). Most VLPs are produced by packaging SpCas9 and its sgRNA, which is expressed from the RNA polymerase III (Pol III)-transcribed U6 promoter. VLPs assemble in the cytoplasm, but U6-driven sgRNA is localized in the nucleus, which hinders the efficient formation and packaging of RNPs into VLPs. In this study, using the nuclease packaging mechanism of ‘NanoMEDIC’ VLPs, we produced VLPs with AsCas12a and exploited its ability to process pre-crRNA. This allowed us t

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Mische, Sarah, Mingang Li, Madeline Serr, and Thomas S. Hays. "Direct Observation of Regulated Ribonucleoprotein Transport Across the Nurse Cell/Oocyte Boundary." Molecular Biology of the Cell 18, no. 6 (2007): 2254–63. http://dx.doi.org/10.1091/mbc.e06-10-0959.

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In Drosophila, the asymmetric localization of specific mRNAs to discrete regions within the developing oocyte determines the embryonic axes. The microtubule motors dynein and kinesin are required for the proper localization of the determinant ribonucleoprotein (RNP) complexes, but the mechanisms that account for RNP transport to and within the oocyte are not well understood. In this work, we focus on the transport of RNA complexes containing bicoid (bcd), an anterior determinant. We show in live egg chambers that, within the nurse cell compartment, dynein actively transports green fluorescent

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Liu, Teresa, and Zhiping Ye. "Introduction of a Temperature-Sensitive Phenotype into Influenza A/WSN/33 Virus by Altering the Basic Amino Acid Domain of Influenza Virus Matrix Protein." Journal of Virology 78, no. 18 (2004): 9585–91. http://dx.doi.org/10.1128/jvi.78.18.9585-9591.2004.

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ABSTRACT Our previous studies with influenza A viruses indicated that the association of M1 with viral RNA and nucleoprotein (NP) is required for the efficient formation of helical ribonucleoprotein (RNP) and for the nuclear export of RNPs. RNA-binding domains of M1 map to the following two independent regions: a zinc finger motif at amino acid positions 148 to 162 and a series of basic amino acids (RKLKR) at amino acid positions 101 to 105. Altering the zinc finger motif of M1 reduces viral growth slightly. A substitution of Ser for Arg at either position 101 or position 105 of the RKLKR doma

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Yang, Pok Kwan, Coralie Hoareau, Carine Froment, Bernard Monsarrat, Yves Henry, and Guillaume Chanfreau. "Cotranscriptional Recruitment of the Pseudouridylsynthetase Cbf5p and of the RNA Binding Protein Naf1p during H/ACA snoRNP Assembly." Molecular and Cellular Biology 25, no. 8 (2005): 3295–304. http://dx.doi.org/10.1128/mcb.25.8.3295-3304.2005.

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ABSTRACT H/ACA small nucleolar ribonucleoprotein particles (snoRNPs) are essential for the maturation and pseudouridylation of the precursor of rRNAs and other stable RNAs. Although the RNA and protein components of these RNPs have been identified, the mechanisms by which they are assembled in vivo are poorly understood. Here we show that the RNA binding protein Naf1p, which is required for H/ACA snoRNPs stability, associates with RNA polymerase II-associated proteins Spt16p, Tfg1p, and Sub1p and with H/ACA snoRNP proteins. Chromatin immunoprecipitation experiments show that Naf1p and the pseu

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Finke, Stefan, Krzysztof Brzózka, and Karl-Klaus Conzelmann. "Tracking Fluorescence-Labeled Rabies Virus: Enhanced Green Fluorescent Protein-Tagged Phosphoprotein P Supports Virus Gene Expression and Formation of Infectious Particles." Journal of Virology 78, no. 22 (2004): 12333–43. http://dx.doi.org/10.1128/jvi.78.22.12333-12343.2004.

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ABSTRACT Rhabdoviruses such as rabies virus (RV) encode only five multifunctional proteins accomplishing viral gene expression and virus formation. The viral phosphoprotein, P, is a structural component of the viral ribonucleoprotein (RNP) complex and an essential cofactor for the viral RNA-dependent RNA polymerase. We show here that RV P fused to enhanced green fluorescent protein (eGFP) can substitute for P throughout the viral life cycle, allowing fluorescence labeling and tracking of RV RNPs under live cell conditions. To first assess the functions of P fusion constructs, a recombinant RV

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Mazurov, Dmitriy, Lama Ramadan, and Natalia Kruglova. "Packaging and Uncoating of CRISPR/Cas Ribonucleoproteins for Efficient Gene Editing with Viral and Non-Viral Extracellular Nanoparticles." Viruses 15, no. 3 (2023): 690. http://dx.doi.org/10.3390/v15030690.

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Rapid progress in gene editing based on clustered regularly interspaced short palindromic repeats/CRISPR-associated protein (CRISPR/Cas) has revolutionized functional genomic studies and genetic disease correction. While numerous gene editing applications have been easily adapted by experimental science, the clinical utility of CRISPR/Cas remains very limited due to difficulty in delivery to primary cells and possible off-target effects. The use of CRISPR in the form of a ribonucleoprotein (RNP) complex substantially reduces the time of DNA exposure to the effector nuclease and minimizes its o

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Dez, Christophe, Jacqueline Noaillac-Depeyre, Michèle Caizergues-Ferrer, and Yves Henry. "Naf1p, an Essential Nucleoplasmic Factor Specifically Required for Accumulation of Box H/ACA Small Nucleolar RNPs." Molecular and Cellular Biology 22, no. 20 (2002): 7053–65. http://dx.doi.org/10.1128/mcb.22.20.7053-7065.2002.

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ABSTRACT Box H/ACA small nucleolar ribonucleoprotein particles (H/ACA snoRNPs) play key roles in the synthesis of eukaryotic ribosomes. The ways in which these particles are assembled and correctly localized in the dense fibrillar component of the nucleolus remain largely unknown. Recently, the essential Saccharomyces cerevisiae Naf1p protein (encoded by the YNL124W open reading frame) was found to interact in a two-hybrid assay with two core protein components of mature H/ACA snoRNPs, Cbf5p and Nhp2p (T. Ito, T. Chiba, R. Ozawa, M. Yoshida, M. Hattori, and Y. Sakaki, Proc. Natl. Acad. Sci. US

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Glätzer, K. H., and P. M. Kloetzel. "Differential chromosomal distribution of ribonucleoprotein antigens in nuclei of Drosophila spermatocytes." Journal of Cell Biology 103, no. 6 (1986): 2113–19. http://dx.doi.org/10.1083/jcb.103.6.2113.

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The ribonucleoprotein (RNP) composition of the active Y chromosomal structures in spermatocyte nuclei of Drosophila hydei has been investigated using the anti-RNP antibodies Dm 28K2 and pp60 as a probe. Antibody Dm 28K2 was raised against an RNP protein of cytoplasmic RNP particles in D. melanogaster cells, while antibody pp60 was raised against a pre-messenger RNP fraction from oocytes of Xenopus laevis. Both antibodies detect nuclear RNP (nRNP) antigens of D. hydei. This is shown by CsCl density centrifugation of nRNP from D. hydei cells and immunoblotting across the density gradient. Dm 28K

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Giorgini, Flaviano, Holly G. Davies, and Robert E. Braun. "MSY2 and MSY4 Bind a Conserved Sequence in the 3′ Untranslated Region of Protamine 1 mRNA In Vitro and In Vivo." Molecular and Cellular Biology 21, no. 20 (2001): 7010–19. http://dx.doi.org/10.1128/mcb.21.20.7010-7019.2001.

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ABSTRACT Y-box proteins are major constituents of ribonucleoprotein particles (RNPs) which contain translationally silent mRNAs in gametic cells. We have recently shown that a sequence-specific RNA binding activity present in spermatogenic cells contains the two Y-box proteins MSY2 and MSY4. We show here that MSY2 and MSY4 bind a sequence, 5′-UCCAUCA-3′, present in the 3′ untranslated region of the translationally repressed protamine 1 (Prm1) mRNA. Using pre- and post-RNase T1-digested substrate RNAs, it was determined that MSY2 and MSY4 can bind an RNA of eight nucleotides containing the MSY2

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Burleigh, Laura M., Lesley J. Calder, John J. Skehel, and David A. Steinhauer. "Influenza A Viruses with Mutations in the M1 Helix Six Domain Display a Wide Variety of Morphological Phenotypes." Journal of Virology 79, no. 2 (2005): 1262–70. http://dx.doi.org/10.1128/jvi.79.2.1262-1270.2005.

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ABSTRACT Several functions required for the replication of influenza A viruses have been attributed to the viral matrix protein (M1), and a number of studies have focused on a region of the M1 protein designated “helix six.” This region contains an exposed positively charged stretch of amino acids, including the motif 101-RKLKR-105, which has been identified as a nuclear localization signal, but several studies suggest that this domain is also involved in functions such as binding to the ribonucleoprotein genome segments (RNPs), membrane association, interaction with the viral nuclear export p

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Brown, Gaie, James Aitken, Helen W. McL Rixon, and Richard J. Sugrue. "Caveolin-1 is incorporated into mature respiratory syncytial virus particles during virus assembly on the surface of virus-infected cells." Journal of General Virology 83, no. 3 (2002): 611–21. http://dx.doi.org/10.1099/0022-1317-83-3-611.

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We have employed immunofluorescence microscopy and transmission electron microscopy to examine the assembly and maturation of respiratory syncytial virus (RSV) in the Vero cell line C1008. RSV matures at the apical cell surface in a filamentous form that extends from the plasma membrane. We observed that inclusion bodies containing viral ribonucleoprotein (RNP) cores predominantly appeared immediately below the plasma membrane, from where RSV filaments form during maturation at the cell surface. A comparison of mock-infected and RSV-infected cells by confocal microscopy revealed a significant

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Schmitt, Phuong Tieu, Greeshma Ray, and Anthony P. Schmitt. "The C-Terminal End of Parainfluenza Virus 5 NP Protein Is Important for Virus-Like Particle Production and M-NP Protein Interaction." Journal of Virology 84, no. 24 (2010): 12810–23. http://dx.doi.org/10.1128/jvi.01885-10.

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ABSTRACT Enveloped virus particles are formed by budding from infected-cell membranes. For paramyxoviruses, viral matrix (M) proteins are key drivers of virus assembly and budding. However, other paramyxovirus proteins, including glycoproteins, nucleocapsid (NP or N) proteins, and C proteins, are also important for particle formation in some cases. To investigate the role of NP protein in parainfluenza virus 5 (PIV5) particle formation, NP protein truncation and substitution mutants were analyzed. Alterations near the C-terminal end of NP protein completely disrupted its virus-like particle (V

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Chan, Wai-Hon, Andy Ka-Leung Ng, Nicole C. Robb, et al. "Functional Analysis of the Influenza Virus H5N1 Nucleoprotein Tail Loop Reveals Amino Acids That Are Crucial for Oligomerization and Ribonucleoprotein Activities." Journal of Virology 84, no. 14 (2010): 7337–45. http://dx.doi.org/10.1128/jvi.02474-09.

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ABSTRACT Homo-oligomerization of the nucleoprotein (NP) of influenza A virus is crucial for providing a major structural framework for the assembly of viral ribonucleoprotein (RNP) particles. The nucleoprotein is also essential for transcription and replication during the virus life cycle. In the H5N1 NP structure, the tail loop region is important for NP to form oligomers. Here, by an RNP reconstitution assay, we identified eight NP mutants that had different degrees of defects in forming functional RNPs, with the RNP activities of four mutants being totally abolished (E339A, V408S P410S, R41

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Agredano-Moreno, Lourdes-Teresa, María De Lourdes Segura-Valdez, Jaime Jiménez-Ramírez, and Luis-Felipe Jiménez-García. "Lacandonia granules are present in the cell nucleus of Welwitschia mirabilis." Botanical Sciences 96, no. 4 (2018): 678. http://dx.doi.org/10.17129/botsci.1924.

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<p><strong>Background:</strong> <em>Lacandonia</em> granules are extranucleolar ribonucleoprotein (RNPs) particles, 32 nanometers in diameter that were first described in the nucleus of <em>Lacandonia schismatica</em>. Cytochemical and immunocytochemical studies suggest that these particles are equivalent to perichromatin and Balbiani ring granules described in mammals and salivary glands cells of the insect <em>Chironomus tentans, </em>respectively. <em>Lacandonia</em> granules are also present in the related <em>Triuris&

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Carotenuto, Pietro, Annalisa Pecoraro, Gaetano Palma, Giulia Russo, and Annapina Russo. "Therapeutic Approaches Targeting Nucleolus in Cancer." Cells 8, no. 9 (2019): 1090. http://dx.doi.org/10.3390/cells8091090.

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The nucleolus is a distinct sub-cellular compartment structure in the nucleus. First observed more than 200 years ago, the nucleolus is detectable by microscopy in eukaryotic cells and visible during the interphase as a sub-nuclear structure immersed in the nucleoplasm, from which it is not separated from any membrane. A huge number of studies, spanning over a century, have identified ribosome biogenesis as the main function of the nucleolus. Recently, novel functions, independent from ribosome biogenesis, have been proposed by several proteomic, genomic, and functional studies. Several works

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Karpova, O. V., O. V. Zayakina, M. V. Arkhipenko, et al. "Potato virus X RNA-mediated assembly of single-tailed ternary ‘coat protein–RNA–movement protein’ complexes." Journal of General Virology 87, no. 9 (2006): 2731–40. http://dx.doi.org/10.1099/vir.0.81993-0.

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Different models have been proposed for the nature of the potexvirus transport form that moves from cell to cell over the infected plant: (i) genomic RNA moves as native virions; or (ii) in vitro-assembled non-virion ribonucleoprotein (RNP) complexes consisting of viral RNA, coat protein (CP) and movement protein (MP), termed TGBp1, serve as the transport form in vivo. As the structure of these RNPs has not been elucidated, the products assembled in vitro from potato virus X (PVX) RNA, CP and TGBp1 were characterized. The complexes appeared as single-tailed particles (STPs) with a helical, hea

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Surtees, Rebecca, Stuart D. Dowall, Amelia Shaw, et al. "Heat Shock Protein 70 Family Members Interact with Crimean-Congo Hemorrhagic Fever Virus and Hazara Virus Nucleocapsid Proteins and Perform a Functional Role in the Nairovirus Replication Cycle." Journal of Virology 90, no. 20 (2016): 9305–16. http://dx.doi.org/10.1128/jvi.00661-16.

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ABSTRACTTheNairovirusgenus of theBunyaviridaefamily contains serious human and animal pathogens classified within multiple serogroups and species. Of these serogroups, the Crimean-Congo hemorrhagic fever virus (CCHFV) serogroup comprises sole members CCHFV and Hazara virus (HAZV). CCHFV is an emerging zoonotic virus that causes often-fatal hemorrhagic fever in infected humans for which preventative or therapeutic strategies are not available. In contrast, HAZV is nonpathogenic to humans and thus represents an excellent model to study aspects of CCHFV biology under conditions of more-accessible

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Boulon, Séverine, Nathalie Marmier-Gourrier, Bérengère Pradet-Balade, et al. "The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery." Journal of Cell Biology 180, no. 3 (2008): 579–95. http://dx.doi.org/10.1083/jcb.200708110.

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RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins (RNPs), including box C/D and H/ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins. In this study, we show that Nufip and its yeast homologue Rsa1 are key components of the machinery that assembles these RNPs. We observed that Rsa1 and Nufip bind several L7Ae proteins and tether them to other core proteins in the immature particles. Surprisingly, Rsa1 and Nufip also link assembling RNPs with the AAA + adenosine triphosphatases hRvb1 and hRvb2 and w

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Yean, S. L., and R. J. Lin. "U4 small nuclear RNA dissociates from a yeast spliceosome and does not participate in the subsequent splicing reaction." Molecular and Cellular Biology 11, no. 11 (1991): 5571–77. http://dx.doi.org/10.1128/mcb.11.11.5571-5577.1991.

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U4 and U6 small nuclear RNAs reside in a single ribonucleoprotein particle, and both are required for pre-mRNA splicing. The U4/U6 and U5 small nuclear ribonucleoproteins join U1 and U2 on the pre-mRNA during spliceosome assembly. Binding of U4 is then destabilized prior to or concomitant with the 5' cleavage-ligation. In order to test the role of U4 RNA, we isolated a functional spliceosome by using extracts prepared from yeast cells carrying a temperature-sensitive allele of prp2 (rna2). The isolated prp2 delta spliceosome contains U2, U5, U6, and possibly also U1 and can be activated to spl

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Yean, S. L., and R. J. Lin. "U4 small nuclear RNA dissociates from a yeast spliceosome and does not participate in the subsequent splicing reaction." Molecular and Cellular Biology 11, no. 11 (1991): 5571–77. http://dx.doi.org/10.1128/mcb.11.11.5571.

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U4 and U6 small nuclear RNAs reside in a single ribonucleoprotein particle, and both are required for pre-mRNA splicing. The U4/U6 and U5 small nuclear ribonucleoproteins join U1 and U2 on the pre-mRNA during spliceosome assembly. Binding of U4 is then destabilized prior to or concomitant with the 5' cleavage-ligation. In order to test the role of U4 RNA, we isolated a functional spliceosome by using extracts prepared from yeast cells carrying a temperature-sensitive allele of prp2 (rna2). The isolated prp2 delta spliceosome contains U2, U5, U6, and possibly also U1 and can be activated to spl

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Malhotra, A., R. K. Tan, and S. C. Harvey. "Modeling large RNAs and ribonucleoprotein particles using molecular mechanics techniques." Biophysical Journal 66, no. 6 (1994): 1777–95. http://dx.doi.org/10.1016/s0006-3495(94)80972-5.

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Överby, Anna K., Vsevolod Popov, Etienne P. A. Neve, and Ralf F. Pettersson. "Generation and Analysis of Infectious Virus-Like Particles of Uukuniemi Virus (Bunyaviridae): a Useful System for Studying Bunyaviral Packaging and Budding." Journal of Virology 80, no. 21 (2006): 10428–35. http://dx.doi.org/10.1128/jvi.01362-06.

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ABSTRACT In the present report we describe an infectious virus-like particle (VLP) system for the Uukuniemi (UUK) virus, a member of the Bunyaviridae family. It utilizes our recently developed reverse genetic system based on the RNA polymerase I minigenome system for UUK virus used to study replication, encapsidation, and transcription by monitoring reporter gene expression. Here, we have added the glycoprotein precursor expression plasmid together with the minigenome, nucleoprotein, and polymerase to generate VLPs, which incorporate the minigenome and are released into the supernatant. The pa

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Galardi, Silvia, Alessandro Fatica, Angela Bachi, Andrea Scaloni, Carlo Presutti, and Irene Bozzoni. "Purified Box C/D snoRNPs Are Able To Reproduce Site-Specific 2′-O-Methylation of Target RNA In Vitro." Molecular and Cellular Biology 22, no. 19 (2002): 6663–68. http://dx.doi.org/10.1128/mcb.22.19.6663-6668.2002.

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ABSTRACT Small nucleolar RNAs (snoRNAs) are associated in ribonucleoprotein particles localized to the nucleolus (snoRNPs). Most of the members of the box C/D family function in directing site-specific 2′-O-methylation of substrate RNAs. Although the selection of the target nucleotide requires the antisense element and the conserved box D or D′ of the snoRNA, the methyltransferase activity is supposed to reside in one of the protein components. Through protein tagging of a snoRNP-specific factor, we purified to homogeneity box C/D snoRNPs from the yeast Saccharomyces cerevisiae. Mass spectrome

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de Lucas, Susana, Joan Peredo, Rosa María Marión, Carmen Sánchez, and Juan Ortín. "Human Staufen1 Protein Interacts with Influenza Virus Ribonucleoproteins and Is Required for Efficient Virus Multiplication." Journal of Virology 84, no. 15 (2010): 7603–12. http://dx.doi.org/10.1128/jvi.00504-10.

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ABSTRACT The influenza A virus genome consists of 8 negative-stranded RNA segments. NS1 is a nonstructural protein that participates in different steps of the virus infectious cycle, including transcription, replication, and morphogenesis, and acts as a virulence factor. Human Staufen1 (hStau1), a protein involved in the transport and regulated translation of cellular mRNAs, was previously identified as a NS1-interacting factor. To investigate the possible role of hStau1 in the influenza virus infection, we characterized the composition of hStau1-containing granules isolated from virus-infecte

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Moran, Steven J., Ryan Oglietti, Kathleen C. Smith, Jed C. Macosko, George Holzwarth, and Douglas S. Lyles. "Mechanisms of active diffusion of vesicular stomatitis virus inclusion bodies and cellular early endosomes in the cytoplasm of mammalian cells." PLOS ONE 19, no. 3 (2024): e0290672. http://dx.doi.org/10.1371/journal.pone.0290672.

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Viral and cellular particles too large to freely diffuse have two different types of mobility in the eukaryotic cell cytoplasm: directed motion mediated by motor proteins moving along cytoskeletal elements with the particle as its load, and motion in random directions mediated by motor proteins interconnecting cytoskeletal elements. The latter motion is referred to as “active diffusion.” Mechanisms of directed motion have been extensively studied compared to mechanisms of active diffusion, despite the observation that active diffusion is more common for many viral and cellular particles. Our p

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Martinez-Salas, Encarnacion, Azman Embarc-Buh, and Rosario Francisco-Velilla. "Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control." International Journal of Molecular Sciences 21, no. 11 (2020): 3868. http://dx.doi.org/10.3390/ijms21113868.

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RNA-binding proteins (RBPs) play a pivotal role in the lifespan of RNAs. The disfunction of RBPs is frequently the cause of cell disorders which are incompatible with life. Furthermore, the ordered assembly of RBPs and RNAs in ribonucleoprotein (RNP) particles determines the function of biological complexes, as illustrated by the survival of the motor neuron (SMN) complex. Defects in the SMN complex assembly causes spinal muscular atrophy (SMA), an infant invalidating disease. This multi-subunit chaperone controls the assembly of small nuclear ribonucleoproteins (snRNPs), which are the critica

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McNally, K. P., and N. Agabian. "Trypanosoma brucei spliced-leader RNA methylations are required for trans splicing in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 4844–51. http://dx.doi.org/10.1128/mcb.12.11.4844-4851.1992.

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The Trypanosoma brucei spliced leader (SL) RNA donates its 5' leader sequence to all nuclear pre-mRNAs via trans RNA splicing. The SL RNA is a small-nuclear U RNA-like molecule which is present in the cell as part of a small ribonucleoprotein particle. However, unlike the trimethylguanosine-capped small nuclear U RNAs, the SL RNA has a highly modified 5' terminus containing an m7G cap and methylations on the first four transcribed nucleotides. Here, we show that incubation of procyclic-form T. brucei in the presence of the S-adenosylmethionine analog, sinefungin, leads to a rapid inhibition of

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McNally, K. P., and N. Agabian. "Trypanosoma brucei spliced-leader RNA methylations are required for trans splicing in vivo." Molecular and Cellular Biology 12, no. 11 (1992): 4844–51. http://dx.doi.org/10.1128/mcb.12.11.4844.

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The Trypanosoma brucei spliced leader (SL) RNA donates its 5' leader sequence to all nuclear pre-mRNAs via trans RNA splicing. The SL RNA is a small-nuclear U RNA-like molecule which is present in the cell as part of a small ribonucleoprotein particle. However, unlike the trimethylguanosine-capped small nuclear U RNAs, the SL RNA has a highly modified 5' terminus containing an m7G cap and methylations on the first four transcribed nucleotides. Here, we show that incubation of procyclic-form T. brucei in the presence of the S-adenosylmethionine analog, sinefungin, leads to a rapid inhibition of

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Spann, P., M. Feinerman, J. Sperling, and R. Sperling. "Isolation and visualization of large compact ribonucleoprotein particles of specific nuclear RNAs." Proceedings of the National Academy of Sciences 86, no. 2 (1989): 466–70. http://dx.doi.org/10.1073/pnas.86.2.466.

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