An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase.
Identifieur interne : 000176 ( Main/Exploration ); précédent : 000175; suivant : 000177An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase.
Auteurs : Iskander M. Ibrahim [États-Unis] ; Huan Wu [États-Unis] ; Roman Ezhov [États-Unis] ; Gilbert E. Kayanja [États-Unis] ; Stanislav D. Zakharov [États-Unis] ; Yanyan Du [États-Unis, République populaire de Chine] ; Weiguo Andy Tao [États-Unis] ; Yulia Pushkar [États-Unis] ; William A. Cramer [États-Unis] ; Sujith Puthiyaveetil [États-Unis]Source :
- Communications biology [ 2399-3642 ] ; 2020.
Abstract
Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.
DOI: 10.1038/s42003-019-0728-4
PubMed: 31925322
PubMed Central: PMC6949291
Affiliations:
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Ibrahim</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Wu, Huan" sort="Wu, Huan" uniqKey="Wu H" first="Huan" last="Wu">Huan Wu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Ezhov, Roman" sort="Ezhov, Roman" uniqKey="Ezhov R" first="Roman" last="Ezhov">Roman Ezhov</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Kayanja, Gilbert E" sort="Kayanja, Gilbert E" uniqKey="Kayanja G" first="Gilbert E" last="Kayanja">Gilbert E. Kayanja</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Zakharov, Stanislav D" sort="Zakharov, Stanislav D" uniqKey="Zakharov S" first="Stanislav D" last="Zakharov">Stanislav D. Zakharov</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Du, Yanyan" sort="Du, Yanyan" uniqKey="Du Y" first="Yanyan" last="Du">Yanyan Du</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author><author><name sortKey="Tao, Weiguo Andy" sort="Tao, Weiguo Andy" uniqKey="Tao W" first="Weiguo Andy" last="Tao">Weiguo Andy Tao</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Pushkar, Yulia" sort="Pushkar, Yulia" uniqKey="Pushkar Y" first="Yulia" last="Pushkar">Yulia Pushkar</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Cramer, William A" sort="Cramer, William A" uniqKey="Cramer W" first="William A" last="Cramer">William A. Cramer</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author><author><name sortKey="Puthiyaveetil, Sujith" sort="Puthiyaveetil, Sujith" uniqKey="Puthiyaveetil S" first="Sujith" last="Puthiyaveetil">Sujith Puthiyaveetil</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA. spveetil@purdue.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907</wicri:regionArea><wicri:noRegion>47907</wicri:noRegion></affiliation></author></analytic><series><title level="j">Communications biology</title><idno type="eISSN">2399-3642</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31925322</PMID><DateRevised><Year>2020</Year><Month>07</Month><Day>09</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2399-3642</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>01</Month><Day>08</Day></PubDate></JournalIssue><Title>Communications biology</Title><ISOAbbreviation>Commun Biol</ISOAbbreviation></Journal><ArticleTitle>An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase.</ArticleTitle><Pagination><MedlinePgn>13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s42003-019-0728-4</ELocationID><Abstract><AbstractText>Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ibrahim</LastName><ForeName>Iskander M</ForeName><Initials>IM</Initials><Identifier Source="ORCID">0000-0002-2744-6307</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Huan</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ezhov</LastName><ForeName>Roman</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kayanja</LastName><ForeName>Gilbert E</ForeName><Initials>GE</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zakharov</LastName><ForeName>Stanislav D</ForeName><Initials>SD</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Du</LastName><ForeName>Yanyan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tao</LastName><ForeName>Weiguo Andy</ForeName><Initials>WA</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pushkar</LastName><ForeName>Yulia</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cramer</LastName><ForeName>William A</ForeName><Initials>WA</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Puthiyaveetil</LastName><ForeName>Sujith</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0001-7505-4511</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA. spveetil@purdue.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>01</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Commun Biol</MedlineTA><NlmUniqueID>101719179</NlmUniqueID><ISSNLinking>2399-3642</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate 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Ibrahim</name></noRegion><name sortKey="Cramer, William A" sort="Cramer, William A" uniqKey="Cramer W" first="William A" last="Cramer">William A. Cramer</name><name sortKey="Du, Yanyan" sort="Du, Yanyan" uniqKey="Du Y" first="Yanyan" last="Du">Yanyan Du</name><name sortKey="Ezhov, Roman" sort="Ezhov, Roman" uniqKey="Ezhov R" first="Roman" last="Ezhov">Roman Ezhov</name><name sortKey="Kayanja, Gilbert E" sort="Kayanja, Gilbert E" uniqKey="Kayanja G" first="Gilbert E" last="Kayanja">Gilbert E. Kayanja</name><name sortKey="Pushkar, Yulia" sort="Pushkar, Yulia" uniqKey="Pushkar Y" first="Yulia" last="Pushkar">Yulia Pushkar</name><name sortKey="Puthiyaveetil, Sujith" sort="Puthiyaveetil, Sujith" uniqKey="Puthiyaveetil S" first="Sujith" last="Puthiyaveetil">Sujith Puthiyaveetil</name><name sortKey="Tao, Weiguo Andy" sort="Tao, Weiguo Andy" uniqKey="Tao W" first="Weiguo Andy" last="Tao">Weiguo Andy Tao</name><name sortKey="Wu, Huan" sort="Wu, Huan" uniqKey="Wu H" first="Huan" last="Wu">Huan Wu</name><name sortKey="Zakharov, Stanislav D" sort="Zakharov, Stanislav D" uniqKey="Zakharov S" first="Stanislav D" last="Zakharov">Stanislav D. Zakharov</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Du, Yanyan" sort="Du, Yanyan" uniqKey="Du Y" first="Yanyan" last="Du">Yanyan Du</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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