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Information available at cut rates: structure and mechanism of ribonucleases
Ribonucleases are counterweights in the balance of gene expression and are also involved in the maturation of functional RNA. Recent structural data reveal how ribonucleases recognize and cleave targets, in most cases with the catalytic assistance of metal cofactors. Many of these enzymes are ‘proce...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Ltd.
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7125677/ https://www.ncbi.nlm.nih.gov/pubmed/17189683 http://dx.doi.org/10.1016/j.sbi.2006.12.001 |
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author | Worrall, Jonathan AR Luisi, Ben F |
author_facet | Worrall, Jonathan AR Luisi, Ben F |
author_sort | Worrall, Jonathan AR |
collection | PubMed |
description | Ribonucleases are counterweights in the balance of gene expression and are also involved in the maturation of functional RNA. Recent structural data reveal how ribonucleases recognize and cleave targets, in most cases with the catalytic assistance of metal cofactors. Many of these enzymes are ‘processive’, in that they make multiple scissions following the binding of substrates; crystallographic data can account for this solution behaviour. These data not only explain how ribonucleases turn over transcripts, but also provide hints about how they often play dual roles in quality control checks on structured RNA. |
format | Online Article Text |
id | pubmed-7125677 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71256772020-04-08 Information available at cut rates: structure and mechanism of ribonucleases Worrall, Jonathan AR Luisi, Ben F Curr Opin Struct Biol Article Ribonucleases are counterweights in the balance of gene expression and are also involved in the maturation of functional RNA. Recent structural data reveal how ribonucleases recognize and cleave targets, in most cases with the catalytic assistance of metal cofactors. Many of these enzymes are ‘processive’, in that they make multiple scissions following the binding of substrates; crystallographic data can account for this solution behaviour. These data not only explain how ribonucleases turn over transcripts, but also provide hints about how they often play dual roles in quality control checks on structured RNA. Elsevier Ltd. 2007-02 2006-12-26 /pmc/articles/PMC7125677/ /pubmed/17189683 http://dx.doi.org/10.1016/j.sbi.2006.12.001 Text en Copyright © 2006 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Worrall, Jonathan AR Luisi, Ben F Information available at cut rates: structure and mechanism of ribonucleases |
title | Information available at cut rates: structure and mechanism of ribonucleases |
title_full | Information available at cut rates: structure and mechanism of ribonucleases |
title_fullStr | Information available at cut rates: structure and mechanism of ribonucleases |
title_full_unstemmed | Information available at cut rates: structure and mechanism of ribonucleases |
title_short | Information available at cut rates: structure and mechanism of ribonucleases |
title_sort | information available at cut rates: structure and mechanism of ribonucleases |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7125677/ https://www.ncbi.nlm.nih.gov/pubmed/17189683 http://dx.doi.org/10.1016/j.sbi.2006.12.001 |
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