Thiol redox-regulation for efficient adjustment of sulfur metabolism in acclimation to abiotic stress.
Identifieur interne : 000098 ( Main/Exploration ); précédent : 000097; suivant : 000099Thiol redox-regulation for efficient adjustment of sulfur metabolism in acclimation to abiotic stress.
Auteurs : Wilena Telman [Allemagne] ; Karl-Josef Dietz [Allemagne]Source :
- Journal of experimental botany [ 1460-2431 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Arabidopsis, Chloroplastes.
- métabolisme : Chloroplastes, Soufre, Thiols.
- physiologie : Arabidopsis.
- Acclimatation, Oxydoréduction, Régulation de l'expression des gènes végétaux, Stress physiologique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Sulfhydryl Compounds, Sulfur.
- genetics : Arabidopsis, Chloroplasts.
- metabolism : Chloroplasts.
- physiology : Arabidopsis.
- Acclimatization, Gene Expression Regulation, Plant, Oxidation-Reduction, Stress, Physiological.
Abstract
Sulfur assimilation and sulfur metabolism are tightly controlled at the transcriptional, post-transcriptional, and post-translational levels in order to meet the demand for reduced sulfur in growth and metabolism. These regulatory mechanisms coordinate the cellular sulfhydryl supply with carbon and nitrogen assimilation in particular. Redox homeostasis is an important cellular parameter intimately connected to sulfur by means of multiple thiol modifications. Post-translational thiol modifications such as disulfide formation, sulfenylation, S-nitrosylation, persulfidation, and S-glutathionylation allow for versatile switching and adjustment of protein functions. This review focuses on redox-regulation of enzymes involved in the sulfur assimilation pathway, namely adenosine 5´-phosphosulfate reductase (APR), adenosine 5´-phosphosulfate kinase (APSK), and γ-glutamylcysteine ligase (GCL). The activity of these enzymes is adjusted at the transcriptional and post-translational level depending on physiological requirements and the state of the redox and reactive oxygen species network, which are tightly linked to abiotic stress conditions. Hormone-dependent fine-tuning contributes to regulation of sulfur assimilation. Thus, the link between oxylipin signalling and sulfur assimilation has been substantiated by identification of the so-called COPS module in the chloroplast with its components cyclophilin 20-3, O-acetylserine thiol lyase, 2-cysteine peroxiredoxin, and serine acetyl transferase. We now have a detailed understanding of how regulation enables the fine-tuning of sulfur assimilation under both normal and abiotic stress conditions.
DOI: 10.1093/jxb/erz118
PubMed: 30868161
Affiliations:
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Dietz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld</wicri:regionArea><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Center for Biotechnology-CeBiTec, Bielefeld University, Universitätsstr. 27, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Center for Biotechnology-CeBiTec, Bielefeld University, Universitätsstr. 27, 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first="Wilena" last="Telman">Wilena Telman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld</wicri:regionArea><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion></affiliation></author><author><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld</wicri:regionArea><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Center for Biotechnology-CeBiTec, Bielefeld University, Universitätsstr. 27, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Center for Biotechnology-CeBiTec, Bielefeld University, Universitätsstr. 27, Bielefeld</wicri:regionArea><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of experimental botany</title><idno type="eISSN">1460-2431</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acclimatization (MeSH)</term><term>Arabidopsis (genetics)</term><term>Arabidopsis (physiology)</term><term>Chloroplasts (genetics)</term><term>Chloroplasts (metabolism)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Stress, Physiological (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acclimatation (MeSH)</term><term>Arabidopsis (génétique)</term><term>Arabidopsis (physiologie)</term><term>Chloroplastes (génétique)</term><term>Chloroplastes (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Soufre (métabolisme)</term><term>Stress physiologique (MeSH)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Sulfhydryl Compounds</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term><term>Chloroplasts</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Chloroplastes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chloroplastes</term><term>Soufre</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acclimatization</term><term>Gene Expression Regulation, Plant</term><term>Oxidation-Reduction</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acclimatation</term><term>Oxydoréduction</term><term>Régulation de l'expression des gènes végétaux</term><term>Stress physiologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sulfur assimilation and sulfur metabolism are tightly controlled at the transcriptional, post-transcriptional, and post-translational levels in order to meet the demand for reduced sulfur in growth and metabolism. These regulatory mechanisms coordinate the cellular sulfhydryl supply with carbon and nitrogen assimilation in particular. Redox homeostasis is an important cellular parameter intimately connected to sulfur by means of multiple thiol modifications. Post-translational thiol modifications such as disulfide formation, sulfenylation, S-nitrosylation, persulfidation, and S-glutathionylation allow for versatile switching and adjustment of protein functions. This review focuses on redox-regulation of enzymes involved in the sulfur assimilation pathway, namely adenosine 5´-phosphosulfate reductase (APR), adenosine 5´-phosphosulfate kinase (APSK), and γ-glutamylcysteine ligase (GCL). The activity of these enzymes is adjusted at the transcriptional and post-translational level depending on physiological requirements and the state of the redox and reactive oxygen species network, which are tightly linked to abiotic stress conditions. Hormone-dependent fine-tuning contributes to regulation of sulfur assimilation. Thus, the link between oxylipin signalling and sulfur assimilation has been substantiated by identification of the so-called COPS module in the chloroplast with its components cyclophilin 20-3, O-acetylserine thiol lyase, 2-cysteine peroxiredoxin, and serine acetyl transferase. We now have a detailed understanding of how regulation enables the fine-tuning of sulfur assimilation under both normal and abiotic stress conditions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30868161</PMID><DateCompleted><Year>2020</Year><Month>07</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1460-2431</ISSN><JournalIssue CitedMedium="Internet"><Volume>70</Volume><Issue>16</Issue><PubDate><Year>2019</Year><Month>08</Month><Day>19</Day></PubDate></JournalIssue><Title>Journal of experimental botany</Title><ISOAbbreviation>J Exp Bot</ISOAbbreviation></Journal><ArticleTitle>Thiol redox-regulation for efficient adjustment of sulfur metabolism in acclimation to abiotic stress.</ArticleTitle><Pagination><MedlinePgn>4223-4236</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/erz118</ELocationID><Abstract><AbstractText>Sulfur assimilation and sulfur metabolism are tightly controlled at the transcriptional, post-transcriptional, and post-translational levels in order to meet the demand for reduced sulfur in growth and metabolism. These regulatory mechanisms coordinate the cellular sulfhydryl supply with carbon and nitrogen assimilation in particular. Redox homeostasis is an important cellular parameter intimately connected to sulfur by means of multiple thiol modifications. Post-translational thiol modifications such as disulfide formation, sulfenylation, S-nitrosylation, persulfidation, and S-glutathionylation allow for versatile switching and adjustment of protein functions. This review focuses on redox-regulation of enzymes involved in the sulfur assimilation pathway, namely adenosine 5´-phosphosulfate reductase (APR), adenosine 5´-phosphosulfate kinase (APSK), and γ-glutamylcysteine ligase (GCL). The activity of these enzymes is adjusted at the transcriptional and post-translational level depending on physiological requirements and the state of the redox and reactive oxygen species network, which are tightly linked to abiotic stress conditions. Hormone-dependent fine-tuning contributes to regulation of sulfur assimilation. Thus, the link between oxylipin signalling and sulfur assimilation has been substantiated by identification of the so-called COPS module in the chloroplast with its components cyclophilin 20-3, O-acetylserine thiol lyase, 2-cysteine peroxiredoxin, and serine acetyl transferase. We now have a detailed understanding of how regulation enables the fine-tuning of sulfur assimilation under both normal and abiotic stress conditions.</AbstractText><CopyrightInformation>© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Telman</LastName><ForeName>Wilena</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dietz</LastName><ForeName>Karl-Josef</ForeName><Initials>KJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, Bielefeld University, Universitätsstr. 25, Bielefeld, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Biotechnology-CeBiTec, Bielefeld University, Universitätsstr. 27, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Exp Bot</MedlineTA><NlmUniqueID>9882906</NlmUniqueID><ISSNLinking>0022-0957</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000064" MajorTopicYN="N">Acclimatization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Arabidopsis thaliana
</Keyword><Keyword MajorTopicYN="Y">chloroplast</Keyword><Keyword MajorTopicYN="Y">redox regulation</Keyword><Keyword MajorTopicYN="Y">sulfur assimilation</Keyword><Keyword MajorTopicYN="Y">sulfur metabolism</Keyword><Keyword MajorTopicYN="Y">thiol regulation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>12</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>03</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>3</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>7</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>3</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30868161</ArticleId><ArticleId IdType="pii">5380414</ArticleId><ArticleId IdType="doi">10.1093/jxb/erz118</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Telman, Wilena" sort="Telman, Wilena" uniqKey="Telman W" first="Wilena" last="Telman">Wilena Telman</name></noRegion><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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