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Lsm proteins and Hfq: Life at the 3′ end
The bacterial Hfq protein is a versatile modulator of RNA function and is particularly important for regulation mediated by small non-coding RNAs. Hfq is a bacterial Sm protein but bears more similarity to the eukaryotic Sm-like (Lsm) family of proteins than the prototypical Sm proteins. Hfq and Lsm...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3710366/ https://www.ncbi.nlm.nih.gov/pubmed/23392247 http://dx.doi.org/10.4161/rna.23695 |
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author | Wilusz, Carol J. Wilusz, Jeffrey |
author_facet | Wilusz, Carol J. Wilusz, Jeffrey |
author_sort | Wilusz, Carol J. |
collection | PubMed |
description | The bacterial Hfq protein is a versatile modulator of RNA function and is particularly important for regulation mediated by small non-coding RNAs. Hfq is a bacterial Sm protein but bears more similarity to the eukaryotic Sm-like (Lsm) family of proteins than the prototypical Sm proteins. Hfq and Lsm proteins share the ability to chaperone RNA-RNA and RNA/protein interactions and an interesting penchant for protecting the 3′ end of a transcript from exonucleolytic decay while encouraging degradation through other pathways. Our view of Lsm function in eukaryotes has historically been informed by studies of Hfq structure and function but mutational analyses and structural studies of Lsm sub-complexes have given important insights as well. Here, we aim to compare and contrast the roles of these evolutionarily related complexes and to highlight areas for future investigation. |
format | Online Article Text |
id | pubmed-3710366 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-37103662013-07-25 Lsm proteins and Hfq: Life at the 3′ end Wilusz, Carol J. Wilusz, Jeffrey RNA Biol Special Focus Review The bacterial Hfq protein is a versatile modulator of RNA function and is particularly important for regulation mediated by small non-coding RNAs. Hfq is a bacterial Sm protein but bears more similarity to the eukaryotic Sm-like (Lsm) family of proteins than the prototypical Sm proteins. Hfq and Lsm proteins share the ability to chaperone RNA-RNA and RNA/protein interactions and an interesting penchant for protecting the 3′ end of a transcript from exonucleolytic decay while encouraging degradation through other pathways. Our view of Lsm function in eukaryotes has historically been informed by studies of Hfq structure and function but mutational analyses and structural studies of Lsm sub-complexes have given important insights as well. Here, we aim to compare and contrast the roles of these evolutionarily related complexes and to highlight areas for future investigation. Landes Bioscience 2013-04-01 2013-02-07 /pmc/articles/PMC3710366/ /pubmed/23392247 http://dx.doi.org/10.4161/rna.23695 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 | Special Focus Review Wilusz, Carol J. Wilusz, Jeffrey Lsm proteins and Hfq: Life at the 3′ end |
title | Lsm proteins and Hfq: Life at the 3′ end |
title_full | Lsm proteins and Hfq: Life at the 3′ end |
title_fullStr | Lsm proteins and Hfq: Life at the 3′ end |
title_full_unstemmed | Lsm proteins and Hfq: Life at the 3′ end |
title_short | Lsm proteins and Hfq: Life at the 3′ end |
title_sort | lsm proteins and hfq: life at the 3′ end |
topic | Special Focus Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3710366/ https://www.ncbi.nlm.nih.gov/pubmed/23392247 http://dx.doi.org/10.4161/rna.23695 |
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