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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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F1000Research
2017
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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. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-5373437 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | F1000Research |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT hallkathleenb rnaandproteinsmutualrespect |