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RNA and Proteins: Mutual Respect

Proteins and RNA are often found in ribonucleoprotein particles (RNPs), where they function in cellular processes to synthesize proteins (the ribosome), chemically modify RNAs (small nucleolar RNPs), splice pre-mRNAs (the spliceosome), and, on a larger scale, sequester RNAs, degrade them, or process...

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Detalles Bibliográficos
Autor principal: Hall, Kathleen B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000Research 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5373437/
https://www.ncbi.nlm.nih.gov/pubmed/28408981
http://dx.doi.org/10.12688/f1000research.10572.1
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author Hall, Kathleen B.
author_facet Hall, Kathleen B.
author_sort Hall, Kathleen B.
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description Proteins and RNA are often found in ribonucleoprotein particles (RNPs), where they function in cellular processes to synthesize proteins (the ribosome), chemically modify RNAs (small nucleolar RNPs), splice pre-mRNAs (the spliceosome), and, on a larger scale, sequester RNAs, degrade them, or process them (P bodies, Cajal bodies, and nucleoli). Each RNA–protein interaction is a story in itself, as both molecules can change conformation, compete for binding sites, and regulate cellular functions. Recent studies of Xist long non-coding RNP, the U4/5/6 tri-small nuclear RNP complex, and an activated state of a spliceosome reveal new features of RNA interactions with proteins, and, although their stories are incomplete, they are already fascinating.
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spelling pubmed-53734372017-04-12 RNA and Proteins: Mutual Respect Hall, Kathleen B. F1000Res Review Proteins and RNA are often found in ribonucleoprotein particles (RNPs), where they function in cellular processes to synthesize proteins (the ribosome), chemically modify RNAs (small nucleolar RNPs), splice pre-mRNAs (the spliceosome), and, on a larger scale, sequester RNAs, degrade them, or process them (P bodies, Cajal bodies, and nucleoli). Each RNA–protein interaction is a story in itself, as both molecules can change conformation, compete for binding sites, and regulate cellular functions. Recent studies of Xist long non-coding RNP, the U4/5/6 tri-small nuclear RNP complex, and an activated state of a spliceosome reveal new features of RNA interactions with proteins, and, although their stories are incomplete, they are already fascinating. F1000Research 2017-03-27 /pmc/articles/PMC5373437/ /pubmed/28408981 http://dx.doi.org/10.12688/f1000research.10572.1 Text en Copyright: © 2017 Hall KB http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Hall, Kathleen B.
RNA and Proteins: Mutual Respect
title RNA and Proteins: Mutual Respect
title_full RNA and Proteins: Mutual Respect
title_fullStr RNA and Proteins: Mutual Respect
title_full_unstemmed RNA and Proteins: Mutual Respect
title_short RNA and Proteins: Mutual Respect
title_sort rna and proteins: mutual respect
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5373437/
https://www.ncbi.nlm.nih.gov/pubmed/28408981
http://dx.doi.org/10.12688/f1000research.10572.1
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