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Annu Rev Biochem. 2014;83:697-725. doi: 10.1146/annurev-biochem-060713-035546. Epub 2014 Mar 12.

RNA helicase proteins as chaperones and remodelers.

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  • 1Department of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712; email: i_jarmoskaite@utexas.edu , rick_russell@cm.utexas.edu.

Abstract

Superfamily 2 helicase proteins are ubiquitous in RNA biology and have an extraordinarily broad set of functional roles. Central among these roles are the promotion of rearrangements of structured RNAs and the remodeling of ribonucleoprotein complexes (RNPs), allowing formation of native RNA structure or progression through a functional cycle of structures. Although all superfamily 2 helicases share a conserved helicase core, they are divided evolutionarily into several families, and it is principally proteins from three families, the DEAD-box, DEAH/RHA, and Ski2-like families, that function to manipulate structured RNAs and RNPs. Strikingly, there are emerging differences in the mechanisms of these proteins, both between families and within the largest family (DEAD-box), and these differences appear to be tuned to their RNA or RNP substrates and their specific roles. This review outlines basic mechanistic features of the three families and surveys individual proteins and the current understanding of their biological substrates and mechanisms.

KEYWORDS:

ATPase; RNA folding; RNA structure; RNA unwinding; self-splicing intron

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