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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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Autores principales: Wilusz, Carol J., Wilusz, Jeffrey
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
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.
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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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