Literature DB >> 12206453

The ubiquitous nature of RNA chaperone proteins.

Gaël Cristofari, Jean-Luc Darlix.   

Abstract

RNA chaperones are ubiquitous and abundant proteins found in all living organisms and viruses, where they interact with various classes of RNA. These highly diverse families of nucleic acid-binding proteins possess activities enabling rapid and faithful RNA-RNA annealing, strand transfer, and exchange and RNA ribozyme-mediated cleavage under physiological conditions. RNA chaperones appear to be critical to functions as important as maintenance of chromosome ends, DNA transcription, preRNA export, splicing and modifications, and mRNA translation and degradation. Here we review some of the properties of RNA chaperones in RNA-RNA interactions that take place during cellular processes and retrovirus replication. Examples of cellular and viral proteins are dicussed vis à vis the relationships between RNA chaperone activities in vitro and functions. In this new "genomic era" we discuss the possible use of small RNA chaperones to improve the synthesis of cDNA libraries for use in large screening reactions using DNA chips.

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Substances:

Year:  2002        PMID: 12206453     DOI: 10.1016/s0079-6603(02)72071-0

Source DB:  PubMed          Journal:  Prog Nucleic Acid Res Mol Biol        ISSN: 0079-6603


  89 in total

1.  FinO is an RNA chaperone that facilitates sense-antisense RNA interactions.

Authors:  David C Arthur; Alexandru F Ghetu; Michael J Gubbins; Ross A Edwards; Laura S Frost; J N Mark Glover
Journal:  EMBO J       Date:  2003-12-01       Impact factor: 11.598

Review 2.  Mechanisms of StpA-mediated RNA remodeling.

Authors:  Martina Doetsch; Thomas Gstrein; Renée Schroeder; Boris Fürtig
Journal:  RNA Biol       Date:  2010-11-01       Impact factor: 4.652

Review 3.  Properties and functions of the nucleocapsid protein in virus assembly.

Authors:  Delphine Muriaux; Jean-Luc Darlix
Journal:  RNA Biol       Date:  2010-11-01       Impact factor: 4.652

4.  The L1Tc C-terminal domain from Trypanosoma cruzi non-long terminal repeat retrotransposon codes for a protein that bears two C2H2 zinc finger motifs and is endowed with nucleic acid chaperone activity.

Authors:  Sara R Heras; Manuel C López; José Luis García-Pérez; Sandra L Martin; M Carmen Thomas
Journal:  Mol Cell Biol       Date:  2005-11       Impact factor: 4.272

5.  The bunyavirus nucleocapsid protein is an RNA chaperone: possible roles in viral RNA panhandle formation and genome replication.

Authors:  M Ayoub Mir; Antonito T Panganiban
Journal:  RNA       Date:  2006-02       Impact factor: 4.942

6.  Dissecting RNA chaperone activity.

Authors:  Lukas Rajkowitsch; Renée Schroeder
Journal:  RNA       Date:  2007-09-27       Impact factor: 4.942

7.  DEAD-box-protein-assisted RNA structure conversion towards and against thermodynamic equilibrium values.

Authors:  Quansheng Yang; Margaret E Fairman; Eckhard Jankowsky
Journal:  J Mol Biol       Date:  2007-03-02       Impact factor: 5.469

8.  A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition.

Authors:  Gaël Cristofari; Carole Bampi; Marcelle Wilhelm; François-Xavier Wilhelm; Jean-Luc Darlix
Journal:  EMBO J       Date:  2002-08-15       Impact factor: 11.598

9.  Distinct nucleic acid interaction properties of HIV-1 nucleocapsid protein precursor NCp15 explain reduced viral infectivity.

Authors:  Wei Wang; Nada Naiyer; Mithun Mitra; Jialin Li; Mark C Williams; Ioulia Rouzina; Robert J Gorelick; Zhengrong Wu; Karin Musier-Forsyth
Journal:  Nucleic Acids Res       Date:  2014-05-09       Impact factor: 16.971

10.  Coronavirus nucleocapsid protein facilitates template switching and is required for efficient transcription.

Authors:  Sonia Zúñiga; Jazmina L G Cruz; Isabel Sola; Pedro A Mateos-Gómez; Lorena Palacio; Luis Enjuanes
Journal:  J Virol       Date:  2009-12-02       Impact factor: 5.103

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