PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli

Detalhes bibliográficos
Autor(a) principal: Dressaire, Clémentine
Data de Publicação: 2018
Outros Autores: Pobre, Vânia, Laguerre, Sandrine, Girbal, Laurence, Arraiano, Cecilia Maria, Cocaign-Bousquet, Muriel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1186/s12864-018-5259-8
Resumo: Background: Exoribonucleases are crucial for RNA degradation in Escherichia coli but the roles of RNase R and PNPase and their potential overlap in stationary phase are not well characterized. Here, we used a genome-wide approach to determine how RNase R and PNPase affect the mRNA half-lives in the stationary phase. The genome-wide mRNA half-lives were determined by a dynamic analysis of transcriptomes after transcription arrest. We have combined the analysis of mRNA half-lives with the steady-state concentrations (transcriptome) to provide an integrated overview of the in vivo activity of these exoribonucleases at the genome-scale. Results: The values of mRNA half-lives demonstrated that the mRNAs are very stable in the stationary phase and that the deletion of RNase R or PNPase caused only a limited mRNA stabilization. Intriguingly the absence of PNPase provoked also the destabilization of many mRNAs. These changes in mRNA half-lives in the PNPase deletion strain were associated with a massive reorganization of mRNA levels and also variation in several ncRNA concentrations. Finally, the in vivo activity of the degradation machinery was found frequently saturated by mRNAs in the PNPase mutant unlike in the RNase R mutant, suggesting that the degradation activity is limited by the deletion of PNPase but not by the deletion of RNase R. Conclusions: This work had identified PNPase as a central player associated with mRNA degradation in stationary phase.
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spelling PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coliE. coliGene expression regulationPNPaseRNA decayRNase RTranscriptomeBiotechnologyGeneticsBackground: Exoribonucleases are crucial for RNA degradation in Escherichia coli but the roles of RNase R and PNPase and their potential overlap in stationary phase are not well characterized. Here, we used a genome-wide approach to determine how RNase R and PNPase affect the mRNA half-lives in the stationary phase. The genome-wide mRNA half-lives were determined by a dynamic analysis of transcriptomes after transcription arrest. We have combined the analysis of mRNA half-lives with the steady-state concentrations (transcriptome) to provide an integrated overview of the in vivo activity of these exoribonucleases at the genome-scale. Results: The values of mRNA half-lives demonstrated that the mRNAs are very stable in the stationary phase and that the deletion of RNase R or PNPase caused only a limited mRNA stabilization. Intriguingly the absence of PNPase provoked also the destabilization of many mRNAs. These changes in mRNA half-lives in the PNPase deletion strain were associated with a massive reorganization of mRNA levels and also variation in several ncRNA concentrations. Finally, the in vivo activity of the degradation machinery was found frequently saturated by mRNAs in the PNPase mutant unlike in the RNase R mutant, suggesting that the degradation activity is limited by the deletion of PNPase but not by the deletion of RNase R. Conclusions: This work had identified PNPase as a central player associated with mRNA degradation in stationary phase.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)Molecular, Structural and Cellular Microbiology (MOSTMICRO)RUNDressaire, ClémentinePobre, VâniaLaguerre, SandrineGirbal, LaurenceArraiano, Cecilia MariaCocaign-Bousquet, Muriel2019-04-26T22:14:13Z2018-11-292018-11-29T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://doi.org/10.1186/s12864-018-5259-8engPURE: 12361305http://www.scopus.com/inward/record.url?scp=85057566097&partnerID=8YFLogxKhttps://doi.org/10.1186/s12864-018-5259-8info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:32:01Zoai:run.unl.pt:10362/67797Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:34:39.857691Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
title PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
spellingShingle PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
Dressaire, Clémentine
E. coli
Gene expression regulation
PNPase
RNA decay
RNase R
Transcriptome
Biotechnology
Genetics
title_short PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
title_full PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
title_fullStr PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
title_full_unstemmed PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
title_sort PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli
author Dressaire, Clémentine
author_facet Dressaire, Clémentine
Pobre, Vânia
Laguerre, Sandrine
Girbal, Laurence
Arraiano, Cecilia Maria
Cocaign-Bousquet, Muriel
author_role author
author2 Pobre, Vânia
Laguerre, Sandrine
Girbal, Laurence
Arraiano, Cecilia Maria
Cocaign-Bousquet, Muriel
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
Molecular, Structural and Cellular Microbiology (MOSTMICRO)
RUN
dc.contributor.author.fl_str_mv Dressaire, Clémentine
Pobre, Vânia
Laguerre, Sandrine
Girbal, Laurence
Arraiano, Cecilia Maria
Cocaign-Bousquet, Muriel
dc.subject.por.fl_str_mv E. coli
Gene expression regulation
PNPase
RNA decay
RNase R
Transcriptome
Biotechnology
Genetics
topic E. coli
Gene expression regulation
PNPase
RNA decay
RNase R
Transcriptome
Biotechnology
Genetics
description Background: Exoribonucleases are crucial for RNA degradation in Escherichia coli but the roles of RNase R and PNPase and their potential overlap in stationary phase are not well characterized. Here, we used a genome-wide approach to determine how RNase R and PNPase affect the mRNA half-lives in the stationary phase. The genome-wide mRNA half-lives were determined by a dynamic analysis of transcriptomes after transcription arrest. We have combined the analysis of mRNA half-lives with the steady-state concentrations (transcriptome) to provide an integrated overview of the in vivo activity of these exoribonucleases at the genome-scale. Results: The values of mRNA half-lives demonstrated that the mRNAs are very stable in the stationary phase and that the deletion of RNase R or PNPase caused only a limited mRNA stabilization. Intriguingly the absence of PNPase provoked also the destabilization of many mRNAs. These changes in mRNA half-lives in the PNPase deletion strain were associated with a massive reorganization of mRNA levels and also variation in several ncRNA concentrations. Finally, the in vivo activity of the degradation machinery was found frequently saturated by mRNAs in the PNPase mutant unlike in the RNase R mutant, suggesting that the degradation activity is limited by the deletion of PNPase but not by the deletion of RNase R. Conclusions: This work had identified PNPase as a central player associated with mRNA degradation in stationary phase.
publishDate 2018
dc.date.none.fl_str_mv 2018-11-29
2018-11-29T00:00:00Z
2019-04-26T22:14:13Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1186/s12864-018-5259-8
url https://doi.org/10.1186/s12864-018-5259-8
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PURE: 12361305
http://www.scopus.com/inward/record.url?scp=85057566097&partnerID=8YFLogxK
https://doi.org/10.1186/s12864-018-5259-8
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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