The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA

As the only oxygenic phototrophs among prokaryotes, cyanobacteria employ intricate mechanisms to regulate common metabolic pathways. These mechanisms include small protein inhibitors exerting their function by protein–protein interaction with key metabolic enzymes and regulatory small RNAs (sRNAs)....

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Detalles Bibliográficos
Autores: Bolay, Paul, Hemm, Luisa, Florencio Bellido, Francisco Javier, Hess, Wolfgang R., Muro Pastor, M. Isabel, Klähn, Stephan
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/139185
Acceso en línea:https://hdl.handle.net/11441/139185
https://doi.org/10.1080/15476286.2022.2082147
Access Level:acceso abierto
Palabra clave:Cyanobacteria
Nitrogen assimilation
Arginine metabolism
RNA regulator
sRNA
Posttranscriptional regulation
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spelling The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirABolay, PaulHemm, LuisaFlorencio Bellido, Francisco JavierHess, Wolfgang R.Muro Pastor, M. IsabelKlähn, StephanCyanobacteriaNitrogen assimilationArginine metabolismRNA regulatorsRNAPosttranscriptional regulationAs the only oxygenic phototrophs among prokaryotes, cyanobacteria employ intricate mechanisms to regulate common metabolic pathways. These mechanisms include small protein inhibitors exerting their function by protein–protein interaction with key metabolic enzymes and regulatory small RNAs (sRNAs). Here we show that the sRNA NsiR4, which is highly expressed under nitrogen limiting conditions, interacts with the mRNA of the recently described small protein PirA in the model strain Synechocystis sp. PCC 6803. In particular, NsiR4 targets the pirA 5ʹUTR close to the ribosome binding site. Heterologous reporter assays confirmed that this interaction interferes with pirA translation. PirA negatively impacts arginine synthesis under ammonium excess by competing with the central carbon/nitrogen regulator PII that binds to and thereby activates the key enzyme of arginine synthesis, N-acetyl-L-glutamate-kinase (NAGK). Consistently, ectopic nsiR4 expression in Synechocystis resulted in lowered PirA accumulation in response to ammonium upshifts, which also affected intracellular arginine pools. As NsiR4 and PirA are inversely regulated by the global nitrogen transcriptional regulator NtcA, this regulatory axis enables fine tuning of arginine synthesis and conveys additional metabolic flexibility under highly fluctuating nitrogen regimes. Pairs of small protein inhibitors and of sRNAs that control the abundance of these enzyme effectors at the post-transcriptional level appear as fundamental building blocks in the regulation of primary metabolism in cyanobacteria.Agencia Estatal de Investigación PID2019-104513GB-100/AEI/10.13039/501100011033German Research Foundation KL3114/2-1, 322977937, KL3114/2-1Taylor & FrancisBioquímica Vegetal y Biología MolecularDeutsche Forschungsgemeinschaft / German Research Foundation (DFG)Agencia Estatal de Investigación. España2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/139185https://doi.org/10.1080/15476286.2022.2082147reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésRNA Biology, 19 (1), 811-818.KL3114/2-1PID2019-104513GB-100/AEI/10.13039/501100011033322977937KL3114/2-1https://doi.org/10.1080/15476286.2022.2082147info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1391852026-06-17T12:51:07Z
dc.title.none.fl_str_mv The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
title The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
spellingShingle The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
Bolay, Paul
Cyanobacteria
Nitrogen assimilation
Arginine metabolism
RNA regulator
sRNA
Posttranscriptional regulation
title_short The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
title_full The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
title_fullStr The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
title_full_unstemmed The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
title_sort The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacterium Synechocystis sp. PCC 6803 by post-transcriptional regulation of PirA
dc.creator.none.fl_str_mv Bolay, Paul
Hemm, Luisa
Florencio Bellido, Francisco Javier
Hess, Wolfgang R.
Muro Pastor, M. Isabel
Klähn, Stephan
author Bolay, Paul
author_facet Bolay, Paul
Hemm, Luisa
Florencio Bellido, Francisco Javier
Hess, Wolfgang R.
Muro Pastor, M. Isabel
Klähn, Stephan
author_role author
author2 Hemm, Luisa
Florencio Bellido, Francisco Javier
Hess, Wolfgang R.
Muro Pastor, M. Isabel
Klähn, Stephan
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Deutsche Forschungsgemeinschaft / German Research Foundation (DFG)
Agencia Estatal de Investigación. España
dc.subject.none.fl_str_mv Cyanobacteria
Nitrogen assimilation
Arginine metabolism
RNA regulator
sRNA
Posttranscriptional regulation
topic Cyanobacteria
Nitrogen assimilation
Arginine metabolism
RNA regulator
sRNA
Posttranscriptional regulation
description As the only oxygenic phototrophs among prokaryotes, cyanobacteria employ intricate mechanisms to regulate common metabolic pathways. These mechanisms include small protein inhibitors exerting their function by protein–protein interaction with key metabolic enzymes and regulatory small RNAs (sRNAs). Here we show that the sRNA NsiR4, which is highly expressed under nitrogen limiting conditions, interacts with the mRNA of the recently described small protein PirA in the model strain Synechocystis sp. PCC 6803. In particular, NsiR4 targets the pirA 5ʹUTR close to the ribosome binding site. Heterologous reporter assays confirmed that this interaction interferes with pirA translation. PirA negatively impacts arginine synthesis under ammonium excess by competing with the central carbon/nitrogen regulator PII that binds to and thereby activates the key enzyme of arginine synthesis, N-acetyl-L-glutamate-kinase (NAGK). Consistently, ectopic nsiR4 expression in Synechocystis resulted in lowered PirA accumulation in response to ammonium upshifts, which also affected intracellular arginine pools. As NsiR4 and PirA are inversely regulated by the global nitrogen transcriptional regulator NtcA, this regulatory axis enables fine tuning of arginine synthesis and conveys additional metabolic flexibility under highly fluctuating nitrogen regimes. Pairs of small protein inhibitors and of sRNAs that control the abundance of these enzyme effectors at the post-transcriptional level appear as fundamental building blocks in the regulation of primary metabolism in cyanobacteria.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/139185
https://doi.org/10.1080/15476286.2022.2082147
url https://hdl.handle.net/11441/139185
https://doi.org/10.1080/15476286.2022.2082147
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv RNA Biology, 19 (1), 811-818.
KL3114/2-1
PID2019-104513GB-100/AEI/10.13039/501100011033
322977937
KL3114/2-1
https://doi.org/10.1080/15476286.2022.2082147
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300719

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