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Ribonucleoprotein (RNP) is a nucleoprotein that contains RNA, i.e. it is an association that combines ribonucleic acid and protein together (referred also as protein-RNA complexes). A few known examples include the ribosome, the enzyme telomerase, vault ribonucleoproteins, RNase P, hnRNP and small nuclear RNPs (snRNPs), which are implicated in pre-mRNA splicing (spliceosome) and are among the main components of the nucleolus.

Currently, over 2000 RNPs can be found in PDB database. Based on known structures some common features of protein-RNA interface were deduced.^[1] For example, RNP in snRNPs has an RNA-binding motif in its RNA-binding protein. Aromatic amino acid residues in this motif result in stacking interactions with RNA. Lysine residues in the helical portion of RNA-binding proteins help to stabilize interactions with nucleic acids. This nucleic acid binding is strengthened by electrostatic attraction between the positive lysine side chains and the negative nucleic acid phosphate backbones. Additionally, it is possible to model RNPs computationally.^[2]

RNPs among many can play an important role in influenza A virus replication. The viral RNA is transcribed into mRNAs by the RNA polymerase attached to the RNPs.^[3]

'RNP' can also refer to ribonucleoprotein particles, distinct intracellular foci for post-transcriptional regulation.

Anti-RNP antibodies

Anti-RNP antibodies are autoantibodies associated with mixed connective tissue disease and are also detected in nearly 40% of Lupus erythematosus patients. Two types of anti-RNP antibodies are closely related to Sjögren's syndrome: SS-A (Ro) and SS-B (La).

List of RNPs

This is a (partial) list of ribonucleoprotein families:

hnRNP
Ribosome
snRNP
Signal recognition particle (a protein coated ribozyme)
Telomerase

References

^ Lewis, B. A.; Walia, R. R.; Terribilini, M; Ferguson, J; Zheng, C; Honavar, V; Dobbs, D (2011). "PRIDB: A Protein-RNA interface database". Nucleic Acids Research 39 (Database issue): D277–82. doi:10.1093/nar/gkq1108. PMC 3013700. PMID 21071426. edit
^ Tuszynska, I; Matelska, D; Magnus, M; Chojnowski, G; Kasprzak, J. M.; Kozlowski, L. P.; Dunin-Horkawicz, S; Bujnicki, J. M. (2014). "Computational modeling of protein-RNA complex structures". Methods 65 (3): 310–9. doi:10.1016/j.ymeth.2013.09.014. PMID 24083976. edit
^ Baudin, F; Bach, C; Cusack, S; Ruigrok, R. W. (1994). "Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent". The EMBO journal 13 (13): 3158–65. PMC 395207. PMID 8039508. edit

External links

Ribonucleoproteins at the US National Library of Medicine Medical Subject Headings (MeSH)
PRIDB Protein-RNA Interface Database

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1. 2本鎖（ds）DNA、Sm、およびU1 RNPに対する抗体 antibodies to double stranded ds dna sm and u1 rnp
2. 混合性結合組織病における抗U1-RNP抗体 anti u1 rnp antibodies in mixed connective tissue disease
3. 混合性結合組織病の臨床症状 clinical manifestations of mixed connective tissue disease
4. 様々な抗核抗体 miscellaneous antinuclear antibodies
5. 混合性結合組織病の定義および診断 definition and diagnosis of mixed connective tissue disease

English Journal

S100A7 overexpression is a predictive marker for high risk of malignant transformation in oral dysplasia.

Kaur J, Matta A, Kak I, Srivastava G, Assi J, Leong I, Witterick I, Colgan TJ, Macmillan C, Siu KW, Walfish PG, Ralhan R.Author information Alex and Simona Shnaider Laboratory in Molecular Oncology, Mount Sinai Hospital, Joseph & Wolf Lebovic Health Complex, Toronto, ON, Canada.AbstractEarly detection of oral lesions (OLs) at high risk of cancer development is of utmost importance for intervention. There is an urgent unmet clinical need for biomarkers that allow identification of high-risk OLs. Recently, we identified and verified a panel of five candidate protein biomarkers namely S100A7, prothymosin alpha, 14-3-3ζ, 14-3-3σ and heterogeneous nuclear ribonucleoprotein K using proteomics to distinguish OLs with dysplasia and oral cancers from normal oral tissues. The objective of our study was to evaluate the potential of these candidate protein biomarkers for identification of oral dysplastic lesions at high risk of cancer development. Using immunohistochemistry, we analyzed expressions of these five candidate protein biomarkers in 110 patients with biopsy-proven oral dysplasia and known clinical outcome and determined their correlations with p16 expression and HPV 16/18 status. Kaplan-Meier survival analysis showed reduced oral cancer-free survival (OCFS) of 68.6 months (p = 0.007) in patients showing cytoplasmic S100A7 overexpression when compared to patients with weak or no S100A7 immunostaining in cytoplasm (mean OCFS = 122.8 months). Multivariate Cox regression analysis revealed cytoplasmic S100A7 overexpression as the most significant candidate marker associated with cancer development in dysplastic lesions (p = 0.041, hazard ratio = 2.36). In conclusion, our study suggested the potential of S100A7 overexpression in identifying OLs with dysplasia at high risk of cancer development.
International journal of cancer. Journal international du cancer.Int J Cancer.2014 Mar 15;134(6):1379-88. doi: 10.1002/ijc.28473. Epub 2013 Oct 8.
Early detection of oral lesions (OLs) at high risk of cancer development is of utmost importance for intervention. There is an urgent unmet clinical need for biomarkers that allow identification of high-risk OLs. Recently, we identified and verified a panel of five candidate protein biomarkers namel
PMID 24122701

Transcriptional analysis of hnRNPA0, A1, A2, B1, and A3 in lung cancer cell lines in response to acidosis, hypoxia, and serum deprivation conditions.

Romero-Garcia S, Prado-Garcia H, Lopez-Gonzalez JS.Author information Department of Chronic-Degenerative Diseases, National Institute of Respiratory Diseases "Ismael Cosío Villegas," Mexico City , Mexico.AbstractABSTRACT The ribonucleoproteins (hnRNPs) have important roles in multiple aspects of nucleic acid metabolism and in the regulation of different cellular processes. Abnormal expression of hnRNPs has been reported in several types of cancer including lung, pancreatic, and gastric carcinomas. Heterogenous tumor cell populations generate a tumor microenvironment that can present normoxic, hypoxic, or acidic regions. The analysis of hnRNP transcriptional responses considering the changing nature of the tumor microenvironment is important to understand tumor cell survival under stress conditions. We analyzed the transcriptional response of hnRNPA0, A1, A2, B1, and A3 in lung tumor cell lines under acidosis, hypoxia, and serum deprivation conditions. We used qRT-PCR to obtain a relative quantification of the hnRNPA/B transcript levels. We found that the hnRNPA2 transcript was the most abundant, followed by B1, A0, and A1. Expression of hnRNPA3 was the lowest, although its transcript levels were the most constant. hnRNPA/B transcript levels in lung tumor cell lines responded to changes in the microenvironment; however, hnRNPB1 transcript levels relative to hnRNPA2 expression did no change in all tested stress conditions, indicating that the alternative splicing between these isoforms was constant. hnRNPA1, A2, and B1 transcript levels were upregulated under serum deprivation conditions; possibly to promote a migration phenotype. Our data provide new insights into the transcriptional responses of ribonucleoproteins that might favor tumor cell survival and migration.
Experimental lung research.Exp Lung Res.2014 Feb;40(1):12-21. doi: 10.3109/01902148.2013.856049. Epub 2013 Nov 18.
ABSTRACT The ribonucleoproteins (hnRNPs) have important roles in multiple aspects of nucleic acid metabolism and in the regulation of different cellular processes. Abnormal expression of hnRNPs has been reported in several types of cancer including lung, pancreatic, and gastric carcinomas. Heterogen
PMID 24246049

Catalytically active telomerase holoenzyme is assembled in the dense fibrillar component of the nucleolus during S phase.

Lee JH, Lee YS, Jeong SA, Khadka P, Roth J, Chung IK.Author information Department of Integrated Omics for Biomedical Science, Graduate School of Yonsei University, 134 Shinchon-dong, Seoul, 120-749, Korea.AbstractThe maintenance of human telomeres requires the ribonucleoprotein enzyme telomerase, which is composed of telomerase reverse transcriptase (TERT), telomerase RNA component, and several additional proteins for assembly and activity. Telomere elongation by telomerase in human cancer cells involves multiple steps including telomerase RNA biogenesis, holoenzyme assembly, intranuclear trafficking, and telomerase recruitment to telomeres. Although telomerase has been shown to accumulate in Cajal bodies for association with telomeric chromatin, it is unclear where and how the assembly and trafficking of catalytically active telomerase is regulated in the context of nuclear architecture. Here, we show that the catalytically active holoenzyme is initially assembled in the dense fibrillar component of the nucleolus during S phase. The telomerase RNP is retained in nucleoli through the interaction of hTERT with nucleolin, a major nucleolar phosphoprotein. Upon association with TCAB1 in S phase, the telomerase RNP is transported from nucleoli to Cajal bodies, suggesting that TCAB1 acts as an S-phase-specific holoenzyme component. Furthermore, depletion of TCAB1 caused an increase in the amount of telomerase RNP associated with nucleolin. These results suggest that the TCAB1-dependent trafficking of telomerase to Cajal bodies occurs in a step separate from the holoenzyme assembly in nucleoli. Thus, we propose that the dense fibrillar component is the provider of active telomerase RNP for supporting the continued proliferation of cancer and stem cells.
Histochemistry and cell biology.Histochem Cell Biol.2014 Feb;141(2):137-52. doi: 10.1007/s00418-013-1166-x. Epub 2013 Dec 7.
The maintenance of human telomeres requires the ribonucleoprotein enzyme telomerase, which is composed of telomerase reverse transcriptase (TERT), telomerase RNA component, and several additional proteins for assembly and activity. Telomere elongation by telomerase in human cancer cells involves mul
PMID 24318571

Japanese Journal

Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis

Shimada Yuko,Burn K. Mahala,Ryusuke Niwa Ryusuke Niwa,Cooley Lynn,丹羽隆介
Developmental biology 355(2), 250-262, 2011-07
… Under nutrient stress, Yps and other components of the oskar ribonucleoprotein complex accumulated in large processing bodies in nurse cells, accompanied by MT reorganization. …
NAID 80021814863

The Contribution of Peripheral Stem-Loops to the Catalytic Activity of Archaeal RNase P RNA from Pyrococcus horikoshii OT3

HARA Tadashi,TERADA Atsushi,YAMAGUCHI Hiroki,NAKASHIMA Takashi,KAKUTA Yoshimitsu,KIMURA Makoto
Bioscience, biotechnology, and biochemistry 75(4), 816-819, 2011-04-23
We investigated the contribution of peripheral stem-loops to the catalytic activity of an archaeal RNase P RNA, PhopRNA, from Pyrococcus horikoshii OT3. PhopRNA mutants, in which the stem-loops were i …
NAID 10028272110

PP-504 Identification of RAM (ribonucleoprotein associated molecule) overexpressed in highgrade prostate cancer cells

庵地孝嗣,田村賢司,降幡睦夫,佐古田初音,川田千明,佐竹宏文,執印太郎
日本泌尿器科學會雜誌 102(2), 488, 2011-03-20
NAID 110008612877

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★リンクテーブル★

リンク元	「リボ核タンパク質」「RNAタンパク質」「RNP」「リボ核蛋白質」
拡張検索	「heteronuclear ribonucleoprotein」「small nuclear ribonucleoprotein」「heterogeneous-nuclear ribonucleoprotein U」「heterogeneous-nuclear ribonucleoprotein group A-B」「heterogeneous-nuclear ribonucleoprotein group F-H」

「リボ核タンパク質」

　　[★]

英: ribonucleoprotein RNP
同: リボ核蛋白質、リボ核蛋白、リボ核タンパク、リボヌクレオタンパク質

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