Ribonucleoprotein particle (RNP)

YRNAs are a class of non-coding RNAs that are components of the Ro60 ribonucleoprotein particle and are essential for initiation of DNA replication. Ro60 ribonucleoprotein particle is a target of autoimmune antibodies in patients suffering from systemic lupus erythematosus and Sjögren’s syndrome. Deregulation of YRNAs has been confirmed in many cancer types, but not in head and neck squamous cell carcinoma (HNSCC). The main aim of this study was to determine the biological role of YRNAs in HNSCC, the expression of YRNAs, and their usefulness as potential HNSCC biomarkers. Using quantitative reverse transcriptase (qRT)-PCR, the expression of YRNAs was measured in HNSCC cell lines, 20 matched cancer tissues, and 70 FFPETs (Formaline-Fixed Paraffin-Embedded Tissue) from HNSCC patients. Using TCGA (The Cancer Genome Atlas) data, an analysis of the expression levels of selected genes, and clinical-pathological parameters was performed. The expression of low and high YRNA1 expressed groups were analysed using gene set enrichment analysis (GSEA). YRNA1 and YRNA5 are significantly downregulated in HNSCC cell lines. YRNA1 was found to be significantly downregulated in patients’ tumour sample. YRNAs were significantly upregulated in T4 stage. YRNA1 showed the highest sensitivity, allowing to distinguish healthy from cancer tissue. An analysis of TCGA data revealed that expression of YRNA1 was significantly altered in the human papilloma virus (HPV) infection status. Patients with medium or high expression of YRNA1 showed better survival outcomes. It was noted that genes correlated with YRNA1 were associated with various processes occurring during cancerogenesis. The GSEA analysis showed high expression enrichment in eight vital processes for cancer development. YRNA1 influence patients’ survival and could be used as an HNSCC biomarker. YRNA1 seems to be a good potential biomarker for HNSCC, however, more studies must be performed and these observations should be verified using an in vitro model.

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Cotranscriptional Recruitment of RNA Exosome Cofactors Rrp47p and Mpp6p and Two Distinct Trf-Air-Mtr4 Polyadenylation (TRAMP) Complexes Assists the Exonuclease Rrp6p in the Targeting and Degradation of an Aberrant Messenger Ribonucleoprotein Particle (mRNP) in Yeast

Journal of Biological Chemistry ◽

10.1074/jbc.m113.491290 ◽

2013 ◽

Vol 288 (44) ◽

pp. 31816-31829 ◽

Cited By ~ 17

Author(s):

Igor Stuparevic ◽

Christine Mosrin-Huaman ◽

Nadège Hervouet-Coste ◽

Mateja Remenaric ◽

A. Rachid Rahmouni

Keyword(s):

Ribonucleoprotein Particle ◽

Messenger Ribonucleoprotein ◽

Rna Exosome

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Is 20S RNA naked?

Molecular and Cellular Biology ◽

10.1128/mcb.11.5.2905 ◽

1991 ◽

Vol 11 (5) ◽

pp. 2905-2908 ◽

Cited By ~ 20

Author(s):

W R Widner ◽

Y Matsumoto ◽

R B Wickner

Keyword(s):

Saccharomyces Cerevisiae ◽

Life Cycle ◽

Heat Shock ◽

Heat Shock Protein ◽

Rna Virus ◽

Circular Rna ◽

Ribonucleoprotein Particle ◽

Multiple Copies

The 20S RNA of Saccharomyces cerevisiae is a single-stranded, circular RNA virus. A previous study suggested that this RNA is part of a 32S ribonucleoprotein particle, being associated with multiple copies of a 23-kilodalton protein. We show here that this protein is, in fact, the chromosome-encoded heat shock protein Hsp26. Furthermore, it is apparently not associated with 20S RNA and plays no obvious role in the life cycle of the virus.

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Identification and characterization of the small nuclear ribonucleoprotein particle D' core protein

Molecular and Cellular Biology ◽

10.1128/mcb.10.9.4480-4485.1990 ◽

1990 ◽

Vol 10 (9) ◽

pp. 4480-4485

Author(s):

J Andersen ◽

R J Feeney ◽

G W Zieve

Keyword(s):

Electrophoretic Mobility ◽

Protein Complexes ◽

Ribonucleoprotein Particle ◽

Small Nuclear Ribonucleoprotein ◽

Core Proteins ◽

Nuclear Ribonucleoprotein ◽

Identification And Characterization ◽

Snrnp Core ◽

Small Nuclear Ribonucleoprotein Particle

The addition of urea to sodium dodecyl sulfate (SDS)-polyacrylamide gels has allowed the identification and characterization of the small nuclear ribonucleoprotein particle (snRNP) D' protein and has also improved resolution of the E, F, and G snRNP core proteins. In standard SDS-polyacrylamide gels, the D' and D snRNP core proteins comigrate at approximately 16 kilodaltons. The addition of urea to the separating gel caused the D' protein to shift to a slower electrophoretic mobility that is distinct from that of the D protein. The shift to a slower electrophoretic mobility in the presence of urea suggests that the D' protein has extensive secondary structure that is not totally disrupted by SDS alone. Both N-terminal sequencing and partial peptide maps indicate that the D and D' proteins are distinct gene products, and the sequence data have identified the faster moving of the two proteins as the previously cloned D protein (L. A. Rokeach, J. A. Haselby, and S. O. Hoch, Proc. Natl. Acad. Sci. USA 85:4832-4836, 1988). In the cytoplasm, the D protein is found primarily in the small-nuclear-RNA-free 6S protein complexes, while the D' protein is found primarily in the 20S protein complexes. Like the D protein, the D' protein is an autoantigen in patients with systemic lupus erythematosus and is recognized by some of the Sm class of autoimmune antisera.

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The Mauriceville plasmid of Neurospora crassa: characterization of a novel reverse transcriptase that begins cDNA synthesis at the 3' end of template RNA

Molecular and Cellular Biology ◽

10.1128/mcb.12.11.5131-5144.1992 ◽

1992 ◽

Vol 12 (11) ◽

pp. 5131-5144

Author(s):

H Wang ◽

J C Kennell ◽

M T Kuiper ◽

J R Sabourin ◽

R Saldanha ◽

...

Keyword(s):

Reverse Transcriptase ◽

Reverse Transcription ◽

Full Length ◽

Minus Strand ◽

Ribonucleoprotein Particle ◽

Cdna Synthesis ◽

Reverse Transcriptases ◽

In Vitro Transcripts

The Mauriceville and Varkud plasmids are retroid elements that propagate in the mitochondria of some Neurospora spp. strains. Previous studies of endogenous reactions in ribonucleoprotein particle preparations suggested that the plasmids use a novel mechanism of reverse transcription that involves synthesis of a full-length minus-strand DNA beginning at the 3' end of the plasmid transcript, which has a 3' tRNA-like structure (M. T. R. Kuiper and A. M. Lambowitz, Cell 55:693-704, 1988). In this study, we developed procedures for releasing the Mauriceville plasmid reverse transcriptase from mitochondrial ribonucleoprotein particles and partially purifying it by heparin-Sepharose chromatography. By using these soluble preparations, we show directly that the Mauriceville plasmid reverse transcriptase synthesizes full-length cDNA copies of in vitro transcripts beginning at the 3' end and has a preference for transcripts having the 3' tRNA-like structure. Further, unlike retroviral reverse transcriptases, the Mauriceville plasmid reverse transcriptase begins cDNA synthesis directly opposite the 3'-terminal nucleotide of the template RNA. The ability to initiate cDNA synthesis directly at the 3' end of template RNAs may also be relevant to the mechanisms of reverse transcription used by LINEs, group II introns, and other non-long terminal repeat retroid elements.

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