Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

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dc.contributor.authorSianidis, G.en
dc.contributor.authorKaramanou, S.en
dc.contributor.authorVrontou, E.en
dc.contributor.authorBoulias, K.en
dc.contributor.authorRepanas, K.en
dc.contributor.authorKyrpides, N.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorEconomou, A.en
dc.date.accessioned2015-11-24T19:26:13Z
dc.date.available2015-11-24T19:26:13Z
dc.identifier.issn0261-4189-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/22704
dc.rightsDefault Licence-
dc.subjectAdenosine Diphosphate/metabolismen
dc.subjectAdenosine Triphosphatases/*chemistry/genetics/*metabolismen
dc.subjectAdenosine Triphosphate/metabolismen
dc.subjectAmino Acid Motifsen
dc.subjectAmino Acid Sequenceen
dc.subjectBacterial Proteins/*chemistry/genetics/*metabolismen
dc.subjectCarrier Proteins/*chemistry/genetics/*metabolismen
dc.subject*Catalytic Domainen
dc.subjectEscherichia coli/*enzymology/genetics/metabolismen
dc.subject*Escherichia coli Proteinsen
dc.subjectGenes, Essential/geneticsen
dc.subjectKineticsen
dc.subject*Membrane Transport Proteinsen
dc.subjectMolecular Sequence Dataen
dc.subjectMutation/geneticsen
dc.subjectProtein Bindingen
dc.subjectProtein Denaturationen
dc.subjectProtein Structure, Secondaryen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Transporten
dc.subjectRecombinant Fusion Proteinsen
dc.subjectTemperatureen
dc.titleCross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA functionen
heal.abstractSecA, the motor subunit of bacterial polypeptide translocase, is an RNA helicase. SecA comprises a dimerization C-terminal domain fused to an ATPase N-terminal domain containing conserved DEAD helicase motifs. We show that the N-terminal domain is organized like the motor core of DEAD proteins, encompassing two subdomains, NBD1 and IRA2. NBD1, a rigid nucleotide-binding domain, contains the minimal ATPase catalytic machinery. IRA2 binds to NBD1 and acts as an intramolecular regulator of ATP hydrolysis by controlling ADP release and optimal ATP catalysis at NBD1. IRA2 is flexible and can undergo changes in its alpha-helical content. The C-terminal domain associates with NBD1 and IRA2 and restricts IRA2 activator function. Thus, cytoplasmic SecA is maintained in the thermally stabilized ADP-bound state and unnecessary ATP hydrolysis cycles are prevented. Two DEAD family motifs in IRA2 are essential for IRA2-NBD1 binding, optimal nucleotide turnover and polypeptide translocation. We propose that translocation ligands alleviate C-terminal domain suppression, allowing IRA2 to stimulate nucleotide turnover at NBD1. DEAD motors may employ similar mechanisms to translocate different enzymes along chemically unrelated biopolymers.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1093/emboj/20.5.961-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11230120-
heal.identifier.secondaryhttp://www.nature.com/emboj/journal/v20/n5/pdf/7593601a.pdf-
heal.journalNameEMBO Jen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2001-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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