Literature DB >> 21045543

Roles of DEAD-box proteins in RNA and RNP Folding.

Cynthia Pan1, Rick Russell.   

Abstract

RNAs and RNA-protein complexes (RNPs) traverse rugged energy landscapes as they fold to their native structures, and many continue to undergo conformational rearrangements as they function. Due to the inherent stability of local RNA structure, proteins are required to assist with RNA conformational transitions during initial folding and in exchange between functional structures. DEAD-box proteins are superfamily 2 RNA helicases that are ubiquitously involved in RNA-mediated processes. Some of these proteins use an ATP-dependent cycle of conformational changes to disrupt RNA structure nonprocessively, accelerating structural transitions of RNAs and RNPs in a manner that bears a strong resemblance to the activities of certain groups of protein chaperones. This review summarizes recent work using model substrates and tractable self-splicing intron RNAs, which has given new insights into how DEAD-box proteins promote RNA folding steps and conformational transitions, and it summarizes recent progress in identifying sites and mechanisms of DEAD-box protein activity within more complex cellular targets.

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Year:  2010        PMID: 21045543      PMCID: PMC3073326          DOI: 10.4161/rna.7.6.13571

Source DB:  PubMed          Journal:  RNA Biol        ISSN: 1547-6286            Impact factor:   4.652


  148 in total

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Authors:  D Herschlag
Journal:  J Biol Chem       Date:  1995-09-08       Impact factor: 5.157

2.  Kinetic intermediates trapped by native interactions in RNA folding.

Authors:  D K Treiber; M S Rook; P P Zarrinkar; J R Williamson
Journal:  Science       Date:  1998-03-20       Impact factor: 47.728

Review 3.  Mechanical devices of the spliceosome: motors, clocks, springs, and things.

Authors:  J P Staley; C Guthrie
Journal:  Cell       Date:  1998-02-06       Impact factor: 41.582

4.  Structural analysis of substrate binding by the molecular chaperone DnaK.

Authors:  X Zhu; X Zhao; W F Burkholder; A Gragerov; C M Ogata; M E Gottesman; W A Hendrickson
Journal:  Science       Date:  1996-06-14       Impact factor: 47.728

5.  New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme.

Authors:  V Lehnert; L Jaeger; F Michel; E Westhof
Journal:  Chem Biol       Date:  1996-12

6.  The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide.

Authors:  J R Lorsch; D Herschlag
Journal:  Biochemistry       Date:  1998-02-24       Impact factor: 3.162

7.  Predicting thermodynamic properties of RNA.

Authors:  M J Serra; D H Turner
Journal:  Methods Enzymol       Date:  1995       Impact factor: 1.600

8.  Kinetics of molecular chaperone action.

Authors:  D Schmid; A Baici; H Gehring; P Christen
Journal:  Science       Date:  1994-02-18       Impact factor: 47.728

9.  Kinetic intermediates in RNA folding.

Authors:  P P Zarrinkar; J R Williamson
Journal:  Science       Date:  1994-08-12       Impact factor: 47.728

10.  RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting.

Authors:  B Sclavi; M Sullivan; M R Chance; M Brenowitz; S A Woodson
Journal:  Science       Date:  1998-03-20       Impact factor: 47.728

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  25 in total

1.  Unwinding the mechanisms of a DEAD-box RNA helicase in cancer.

Authors:  Rick Russell
Journal:  J Mol Biol       Date:  2015-03-30       Impact factor: 5.469

2.  The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins.

Authors:  Selma Sinan; Xiaoyan Yuan; Rick Russell
Journal:  J Biol Chem       Date:  2011-08-30       Impact factor: 5.157

Review 3.  Mitochondrial ribosome assembly in health and disease.

Authors:  Dasmanthie De Silva; Ya-Ting Tu; Alexey Amunts; Flavia Fontanesi; Antoni Barrientos
Journal:  Cell Cycle       Date:  2015-06-01       Impact factor: 4.534

4.  ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo.

Authors:  Jeffrey P Potratz; Mark Del Campo; Rachel Z Wolf; Alan M Lambowitz; Rick Russell
Journal:  J Mol Biol       Date:  2011-06-07       Impact factor: 5.469

Review 5.  RNA helicase proteins as chaperones and remodelers.

Authors:  Inga Jarmoskaite; Rick Russell
Journal:  Annu Rev Biochem       Date:  2014-03-12       Impact factor: 23.643

6.  Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions.

Authors:  Aparna Kishor; Elizabeth J F White; Aerielle E Matsangos; Zisui Yan; Bishal Tandukar; Gerald M Wilson
Journal:  J Biol Chem       Date:  2017-07-05       Impact factor: 5.157

7.  The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.

Authors:  Olga Fedorova; Anna Marie Pyle
Journal:  J Mol Biol       Date:  2012-06-13       Impact factor: 5.469

8.  RNA catalysis as a probe for chaperone activity of DEAD-box helicases.

Authors:  Jeffrey P Potratz; Rick Russell
Journal:  Methods Enzymol       Date:  2012       Impact factor: 1.600

9.  Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.

Authors:  Wenxiang Cao; Maria Magdalena Coman; Steve Ding; Arnon Henn; Elizabeth R Middleton; Michael J Bradley; Elizabeth Rhoades; David D Hackney; Anna Marie Pyle; Enrique M De La Cruz
Journal:  J Mol Biol       Date:  2011-04-09       Impact factor: 5.469

10.  The cellular decapping activators LSm1, Pat1, and Dhh1 control the ratio of subgenomic to genomic Flock House virus RNAs.

Authors:  Mireia Giménez-Barcons; Isabel Alves-Rodrigues; Jennifer Jungfleisch; Priscilla M Van Wynsberghe; Paul Ahlquist; Juana Díez
Journal:  J Virol       Date:  2013-03-27       Impact factor: 5.103

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