RNA chaperones buffer deleterious mutations in E. coli
Both proteins and RNAs can misfold into non-functional conformations. Protein chaperones promote native folding of nascent polypeptides and refolding of misfolded species, thereby buffering mutations that compromise protein structure and function. Here, we show that RNA chaperones can also act as mu...
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eLife Sciences Publications, Ltd
2015
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Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4402597/ |
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pubmed-44025972015-04-22 RNA chaperones buffer deleterious mutations in E. coli Rudan, Marina Schneider, Dominique Warnecke, Tobias Krisko, Anita Genomics and Evolutionary Biology Both proteins and RNAs can misfold into non-functional conformations. Protein chaperones promote native folding of nascent polypeptides and refolding of misfolded species, thereby buffering mutations that compromise protein structure and function. Here, we show that RNA chaperones can also act as mutation buffers that enhance organismal fitness. Using competition assays, we demonstrate that overexpression of select RNA chaperones, including three DEAD box RNA helicases (DBRHs) (CsdA, SrmB, RhlB) and the cold shock protein CspA, improves fitness of two independently evolved Escherichia coli mutator strains that have accumulated deleterious mutations during short- and long-term laboratory evolution. We identify strain-specific mutations that are deleterious and subject to buffering when introduced individually into the ancestral genotype. For DBRHs, we show that buffering requires helicase activity, implicating RNA structural remodelling in the buffering process. Our results suggest that RNA chaperones might play a fundamental role in RNA evolution and evolvability. eLife Sciences Publications, Ltd 2015-03-25 /pmc/articles/PMC4402597/ /pubmed/25806682 http://dx.doi.org/10.7554/eLife.04745 Text en © 2015, Rudan et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Rudan, Marina Schneider, Dominique Warnecke, Tobias Krisko, Anita |
spellingShingle |
Rudan, Marina Schneider, Dominique Warnecke, Tobias Krisko, Anita RNA chaperones buffer deleterious mutations in E. coli |
author_facet |
Rudan, Marina Schneider, Dominique Warnecke, Tobias Krisko, Anita |
author_sort |
Rudan, Marina |
title |
RNA chaperones buffer deleterious mutations in E. coli |
title_short |
RNA chaperones buffer deleterious mutations in E. coli |
title_full |
RNA chaperones buffer deleterious mutations in E. coli |
title_fullStr |
RNA chaperones buffer deleterious mutations in E. coli |
title_full_unstemmed |
RNA chaperones buffer deleterious mutations in E. coli |
title_sort |
rna chaperones buffer deleterious mutations in e. coli |
description |
Both proteins and RNAs can misfold into non-functional conformations. Protein chaperones promote native folding of nascent polypeptides and refolding of misfolded species, thereby buffering mutations that compromise protein structure and function. Here, we show that RNA chaperones can also act as mutation buffers that enhance organismal fitness. Using competition assays, we demonstrate that overexpression of select RNA chaperones, including three DEAD box RNA helicases (DBRHs) (CsdA, SrmB, RhlB) and the cold shock protein CspA, improves fitness of two independently evolved Escherichia coli mutator strains that have accumulated deleterious mutations during short- and long-term laboratory evolution. We identify strain-specific mutations that are deleterious and subject to buffering when introduced individually into the ancestral genotype. For DBRHs, we show that buffering requires helicase activity, implicating RNA structural remodelling in the buffering process. Our results suggest that RNA chaperones might play a fundamental role in RNA evolution and evolvability. |
publisher |
eLife Sciences Publications, Ltd |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4402597/ |
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1613213283208134656 |