Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis
Identifieur interne : 000287 ( Pmc/Checkpoint ); précédent : 000286; suivant : 000288Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis
Auteurs : Tatyana A. Sysoeva [États-Unis] ; Saikat Chowdhury [États-Unis] ; Liang Guo [États-Unis] ; B. Tracy Nixon [États-Unis]Source :
- Genes & Development [ 0890-9369 ] ; 2013.
Abstract
AAA+ ATPase molecular machines perform mechanical work in all organisms. A key question is how rings of identical subunits interact with asymmetric target macromolecules. This study by Nixon and colleagues elucidates the structure of AAA+ ATPase bacterial transcriptional activator NtrC1, providing mechanistic insight into transcription initiation. Partial ATP occupancy causes the heptameric closed ring of NtrC1 to rearrange into a hexameric split ring of striking asymmetry. Furthermore, the similarity between the structure of NtrC1 and those of distantly related helicases reveals a general mechanism for homomeric ATPase function.
Url:
DOI: 10.1101/gad.229385.113
PubMed: 24240239
PubMed Central: 3841738
Affiliations:
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Sysoeva</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Chowdhury, Saikat" sort="Chowdhury, Saikat" uniqKey="Chowdhury S" first="Saikat" last="Chowdhury">Saikat Chowdhury</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Guo, Liang" sort="Guo, Liang" uniqKey="Guo L" first="Liang" last="Guo">Liang Guo</name><affiliation wicri:level="1"><nlm:aff id="aff2">BioCAT at Advanced Photon Source/Argonne National Laboratory, Illinois Institute of Technology, Argonne, Illinois 60439, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>BioCAT at Advanced Photon Source/Argonne National Laboratory, Illinois Institute of Technology, Argonne, Illinois 60439</wicri:regionArea><wicri:noRegion>Illinois 60439</wicri:noRegion></affiliation></author><author><name sortKey="Nixon, B Tracy" sort="Nixon, B Tracy" uniqKey="Nixon B" first="B. Tracy" last="Nixon">B. Tracy Nixon</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24240239</idno><idno type="pmc">3841738</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3841738</idno><idno type="RBID">PMC:3841738</idno><idno type="doi">10.1101/gad.229385.113</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000360</idno><idno type="wicri:Area/Pmc/Curation">000360</idno><idno type="wicri:Area/Pmc/Checkpoint">000287</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis</title><author><name sortKey="Sysoeva, Tatyana A" sort="Sysoeva, Tatyana A" uniqKey="Sysoeva T" first="Tatyana A." last="Sysoeva">Tatyana A. Sysoeva</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Chowdhury, Saikat" sort="Chowdhury, Saikat" uniqKey="Chowdhury S" first="Saikat" last="Chowdhury">Saikat Chowdhury</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Guo, Liang" sort="Guo, Liang" uniqKey="Guo L" first="Liang" last="Guo">Liang Guo</name><affiliation wicri:level="1"><nlm:aff id="aff2">BioCAT at Advanced Photon Source/Argonne National Laboratory, Illinois Institute of Technology, Argonne, Illinois 60439, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>BioCAT at Advanced Photon Source/Argonne National Laboratory, Illinois Institute of Technology, Argonne, Illinois 60439</wicri:regionArea><wicri:noRegion>Illinois 60439</wicri:noRegion></affiliation></author><author><name sortKey="Nixon, B Tracy" sort="Nixon, B Tracy" uniqKey="Nixon B" first="B. Tracy" last="Nixon">B. Tracy Nixon</name><affiliation wicri:level="4"><nlm:aff id="aff1">Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</wicri:regionArea><orgName type="university">Université d'État de Pennsylvanie</orgName><placeName><settlement type="city">University Park (Pennsylvanie)</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author></analytic><series><title level="j">Genes & Development</title><idno type="ISSN">0890-9369</idno><idno type="eISSN">1549-5477</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>AAA<sup>+</sup> ATPase molecular machines perform mechanical work in all organisms. A key question is how rings of identical subunits interact with asymmetric target macromolecules. This study by Nixon and colleagues elucidates the structure of AAA<sup>+</sup> ATPase bacterial transcriptional activator NtrC1, providing mechanistic insight into transcription initiation. Partial ATP occupancy causes the heptameric closed ring of NtrC1 to rearrange into a hexameric split ring of striking asymmetry. Furthermore, the similarity between the structure of NtrC1 and those of distantly related helicases reveals a general mechanism for homomeric ATPase function.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Genes Dev</journal-id><journal-id journal-id-type="iso-abbrev">Genes Dev</journal-id><journal-id journal-id-type="publisher-id">GAD</journal-id><journal-title-group><journal-title>Genes & Development</journal-title></journal-title-group><issn pub-type="ppub">0890-9369</issn><issn pub-type="epub">1549-5477</issn><publisher><publisher-name>Cold Spring Harbor Laboratory Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">24240239</article-id><article-id pub-id-type="pmc">3841738</article-id><article-id pub-id-type="medline">8711660</article-id><article-id pub-id-type="doi">10.1101/gad.229385.113</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Paper</subject></subj-group></article-categories><title-group><article-title>Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis</article-title><alt-title alt-title-type="left-running">Sysoeva et al.</alt-title><alt-title alt-title-type="right-running">Crucial asymmetry in bEBP ATPase ring</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Sysoeva</surname><given-names>Tatyana A.</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="author-notes" rid="fn1">3</xref><xref ref-type="author-notes" rid="fn2">4</xref></contrib><contrib contrib-type="author"><name><surname>Chowdhury</surname><given-names>Saikat</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="author-notes" rid="fn1">3</xref><xref ref-type="author-notes" rid="fn3">5</xref></contrib><contrib contrib-type="author"><name><surname>Guo</surname><given-names>Liang</given-names></name><xref ref-type="aff" rid="aff2">2</xref></contrib><contrib contrib-type="author"><name><surname>Nixon</surname><given-names>B. Tracy</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="corresp" rid="cor1">6</xref></contrib><aff id="aff1"><label>1</label>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA;</aff><aff id="aff2"><label>2</label>BioCAT at Advanced Photon Source/Argonne National Laboratory, Illinois Institute of Technology, Argonne, Illinois 60439, USA</aff></contrib-group><author-notes><fn fn-type="equal" id="fn1"><label>3</label><p>These authors contributed equally to this work.</p></fn><fn fn-type="present-address" id="fn2"><p>Present addresses: <sup>4</sup>Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Ave., Cambridge, MA 02138, USA;</p></fn><fn fn-type="present-address" id="fn3"><label>5</label><p>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037, USA</p></fn><corresp id="cor1"><label>6</label>Corresponding author E-mail <email xlink:type="simple">btn1@psu.edu</email></corresp></author-notes><pub-date pub-type="ppub"><day>15</day><month>11</month><year>2013</year></pub-date><volume>27</volume><issue>22</issue><fpage>2500</fpage><lpage>2511</lpage><history><date date-type="received"><day>25</day><month>8</month><year>2013</year></date><date date-type="accepted"><day>16</day><month>10</month><year>2013</year></date></history><permissions><copyright-statement><ext-link ext-link-type="uri" xlink:href="http://genesdev.cshlp.org/site/misc/terms.xhtml">© 2013 Sysoeva et al.; Published by Cold Spring Harbor Laboratory Press</ext-link></copyright-statement><copyright-year>2013</copyright-year><license license-type="creative-commons" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/"><license-p>This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see <ext-link ext-link-type="uri" xlink:href="http://genesdev.cshlp.org/site/misc/terms.xhtml">http://genesdev.cshlp.org/site/misc/terms.xhtml</ext-link>). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/">http://creativecommons.org/licenses/by-nc/3.0/</ext-link>.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="2500.pdf"></self-uri><abstract abstract-type="precis"><p>AAA<sup>+</sup> ATPase molecular machines perform mechanical work in all organisms. A key question is how rings of identical subunits interact with asymmetric target macromolecules. This study by Nixon and colleagues elucidates the structure of AAA<sup>+</sup> ATPase bacterial transcriptional activator NtrC1, providing mechanistic insight into transcription initiation. Partial ATP occupancy causes the heptameric closed ring of NtrC1 to rearrange into a hexameric split ring of striking asymmetry. Furthermore, the similarity between the structure of NtrC1 and those of distantly related helicases reveals a general mechanism for homomeric ATPase function.</p></abstract><abstract><p>It is largely unknown how the typical homomeric ring geometry of ATPases associated with various cellular activities enables them to perform mechanical work. Small-angle solution X-ray scattering, crystallography, and electron microscopy (EM) reconstructions revealed that partial ATP occupancy caused the heptameric closed ring of the bacterial enhancer-binding protein (bEBP) NtrC1 to rearrange into a hexameric split ring of striking asymmetry. The highly conserved and functionally crucial GAFTGA loops responsible for interacting with σ54–RNA polymerase formed a spiral staircase. We propose that splitting of the ensemble directs ATP hydrolysis within the oligomer, and the ring's asymmetry guides interaction between ATPase and the complex of σ54 and promoter DNA. Similarity between the structure of the transcriptional activator NtrC1 and those of distantly related helicases Rho and E1 reveals a general mechanism in homomeric ATPases whereby complex allostery within the ring geometry forms asymmetric functional states that allow these biological motors to exert directional forces on their target macromolecules.</p></abstract><kwd-group><kwd>AAA<sup>+</sup> ATPase</kwd><kwd>mechanochemical ATPases</kwd><kwd>multimeric ATPases</kwd><kwd>bacterial enhancer-binding protein (bEBP)</kwd><kwd>σ54-dependent transcription</kwd><kwd>σ54-dependent transcription activators</kwd></kwd-group><counts><page-count count="12"></page-count></counts></article-meta></front></pmc><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>University Park (Pennsylvanie)</li></settlement><orgName><li>Université d'État de Pennsylvanie</li></orgName></list><tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Sysoeva, Tatyana A" sort="Sysoeva, Tatyana A" uniqKey="Sysoeva T" first="Tatyana A." last="Sysoeva">Tatyana A. Sysoeva</name></region><name sortKey="Chowdhury, Saikat" sort="Chowdhury, Saikat" uniqKey="Chowdhury S" first="Saikat" last="Chowdhury">Saikat Chowdhury</name><name sortKey="Guo, Liang" sort="Guo, Liang" uniqKey="Guo L" first="Liang" last="Guo">Liang Guo</name><name sortKey="Nixon, B Tracy" sort="Nixon, B Tracy" uniqKey="Nixon B" first="B. Tracy" last="Nixon">B. Tracy Nixon</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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