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Toward a molecular understanding of RNA remodeling by DEAD-box proteins
DEAD-box proteins are superfamily 2 helicases that function in all aspects of RNA metabolism. They employ ATP binding and hydrolysis to generate tight, yet regulated RNA binding, which is used to unwind short RNA helices non-processively and promote structural transitions of RNA and RNA-protein subs...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3590237/ https://www.ncbi.nlm.nih.gov/pubmed/22995827 http://dx.doi.org/10.4161/rna.22210 |
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author | Russell, Rick Jarmoskaite, Inga Lambowitz, Alan M. |
author_facet | Russell, Rick Jarmoskaite, Inga Lambowitz, Alan M. |
author_sort | Russell, Rick |
collection | PubMed |
description | DEAD-box proteins are superfamily 2 helicases that function in all aspects of RNA metabolism. They employ ATP binding and hydrolysis to generate tight, yet regulated RNA binding, which is used to unwind short RNA helices non-processively and promote structural transitions of RNA and RNA-protein substrates. In the last few years, substantial progress has been made toward a detailed, quantitative understanding of the structural and biochemical properties of DEAD-box proteins. Concurrently, progress has been made toward a physical understanding of the RNA rearrangements and folding steps that are accelerated by DEAD-box proteins in model systems. Here, we review the recent progress on both of these fronts, focusing on the mitochondrial DEAD-box proteins Mss116 and CYT-19 and their mechanisms in promoting the splicing of group I and group II introns. |
format | Online Article Text |
id | pubmed-3590237 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-35902372013-04-09 Toward a molecular understanding of RNA remodeling by DEAD-box proteins Russell, Rick Jarmoskaite, Inga Lambowitz, Alan M. RNA Biol Review DEAD-box proteins are superfamily 2 helicases that function in all aspects of RNA metabolism. They employ ATP binding and hydrolysis to generate tight, yet regulated RNA binding, which is used to unwind short RNA helices non-processively and promote structural transitions of RNA and RNA-protein substrates. In the last few years, substantial progress has been made toward a detailed, quantitative understanding of the structural and biochemical properties of DEAD-box proteins. Concurrently, progress has been made toward a physical understanding of the RNA rearrangements and folding steps that are accelerated by DEAD-box proteins in model systems. Here, we review the recent progress on both of these fronts, focusing on the mitochondrial DEAD-box proteins Mss116 and CYT-19 and their mechanisms in promoting the splicing of group I and group II introns. Landes Bioscience 2013-01-01 /pmc/articles/PMC3590237/ /pubmed/22995827 http://dx.doi.org/10.4161/rna.22210 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Review Russell, Rick Jarmoskaite, Inga Lambowitz, Alan M. Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title | Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title_full | Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title_fullStr | Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title_full_unstemmed | Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title_short | Toward a molecular understanding of RNA remodeling by DEAD-box proteins |
title_sort | toward a molecular understanding of rna remodeling by dead-box proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3590237/ https://www.ncbi.nlm.nih.gov/pubmed/22995827 http://dx.doi.org/10.4161/rna.22210 |
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