Literature DB >> 18342629

RNA-binding proteins and post-transcriptional gene regulation.

Tina Glisovic1, Jennifer L Bachorik, Jeongsik Yong, Gideon Dreyfuss.   

Abstract

RNAs in cells are associated with RNA-binding proteins (RBPs) to form ribonucleoprotein (RNP) complexes. The RBPs influence the structure and interactions of the RNAs and play critical roles in their biogenesis, stability, function, transport and cellular localization. Eukaryotic cells encode a large number of RBPs (thousands in vertebrates), each of which has unique RNA-binding activity and protein-protein interaction characteristics. The remarkable diversity of RBPs, which appears to have increased during evolution in parallel to the increase in the number of introns, allows eukaryotic cells to utilize them in an enormous array of combinations giving rise to a unique RNP for each RNA. In this short review, we focus on the RBPs that interact with pre-mRNAs and mRNAs and discuss their roles in the regulation of post-transcriptional gene expression.

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Year:  2008        PMID: 18342629      PMCID: PMC2858862          DOI: 10.1016/j.febslet.2008.03.004

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  132 in total

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Journal:  Curr Biol       Date:  2003-02-04       Impact factor: 10.834

2.  Functional coupling of last-intron splicing and 3'-end processing to transcription in vitro: the poly(A) signal couples to splicing before committing to cleavage.

Authors:  Frank Rigo; Harold G Martinson
Journal:  Mol Cell Biol       Date:  2007-10-29       Impact factor: 4.272

3.  HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal.

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4.  NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C.

Authors:  M Inoue; Y Muto; H Sakamoto; S Yokoyama
Journal:  Nucleic Acids Res       Date:  2000-04-15       Impact factor: 16.971

5.  Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription.

Authors:  G Dreyfuss; S A Adam; Y D Choi
Journal:  Mol Cell Biol       Date:  1984-03       Impact factor: 4.272

6.  Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies.

Authors:  G Dreyfuss; Y D Choi; S A Adam
Journal:  Mol Cell Biol       Date:  1984-06       Impact factor: 4.272

7.  Y14 and hUpf3b form an NMD-activating complex.

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Review 8.  Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs.

Authors:  A Gregory Matera; Rebecca M Terns; Michael P Terns
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9.  Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.

Authors:  Corey R Mandel; Syuzo Kaneko; Hailong Zhang; Damara Gebauer; Vasupradha Vethantham; James L Manley; Liang Tong
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10.  A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay.

Authors:  Maria A Ferraiuolo; Chung-Sheng Lee; Lian Wee Ler; Jeanne L Hsu; Mauro Costa-Mattioli; Ming-Juan Luo; Robin Reed; Nahum Sonenberg
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  552 in total

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2.  EgRBP42 encoding an hnRNP-like RNA-binding protein from Elaeis guineensis Jacq. is responsive to abiotic stresses.

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Review 3.  Spotlight on post-transcriptional control in the circadian system.

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Journal:  Cell Mol Life Sci       Date:  2010-08-30       Impact factor: 9.261

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5.  RNase-assisted RNA chromatography.

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6.  Characterization and expression of lin-28a involved in lin28/let-7signal pathway during early development of P. olivaceus.

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Review 7.  Structural and functional characteristics of oestrogen receptor β splice variants: Implications for the ageing brain.

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8.  RNA-binding motif protein 35A is a novel tumor suppressor for colorectal cancer.

Authors:  Olga V Leontieva; Yuri Ionov
Journal:  Cell Cycle       Date:  2009-02-22       Impact factor: 4.534

9.  PAR-CLIP (Photoactivatable Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation): a step-by-step protocol to the transcriptome-wide identification of binding sites of RNA-binding proteins.

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10.  RIPiT-Seq: a high-throughput approach for footprinting RNA:protein complexes.

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