Stabilization of G Domain Conformations in the tRNA-modifying MnmE-GidA Complex Observed with Double Electron Electron Resonance Spectroscopy
DC Element | Wert | Sprache |
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dc.contributor.author | Boehme, Sabine | |
dc.contributor.author | Meyer, Simon | |
dc.contributor.author | Krueger, Andre | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.contributor.author | Wittinghofer, Alfred | |
dc.contributor.author | Klare, Johann P. | |
dc.date.accessioned | 2021-12-23T16:07:56Z | - |
dc.date.available | 2021-12-23T16:07:56Z | - |
dc.date.issued | 2010 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/8142 | - |
dc.description.abstract | MnmE is a GTP-binding protein conserved between bacteria and eukarya. It is a dimeric three-domain protein where the two G domains have to approach each other for activation of the potassium-stimulated GTPase reaction. Together with GidA, in a heterotetrameric alpha(2)beta(2) complex, it is involved in the modification of the wobble uridine base U34 of the first anticodon position of particular tRNAs. Here we show, using various spin-labeled MnmE mutants and EPR spectroscopy, that GidA binding induces large conformational and dynamic changes in MnmE. It stimulates the GTPase reaction by stabilizing the GTP-bound conformation in a potassium-independent manner. Surprisingly, GidA binding influences not only the GTP-but also the GDP-bound conformation. Thus GidA is a new type of regulator for a G protein activated by dimerization. | |
dc.description.sponsorship | Fond der Chemischen IndustrieFonds der Chemischen Industrie; International Max-Planck Research School; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [STE640/7-2]; Graduate College [612]; This work was supported by funds from the Fond der Chemischen Industrie (to S.M.) and the International Max-Planck Research School (to S.M.), Deutsche Forschungsgemeinschaft Grant STE640/7-2 (to S.B., J.P.K., and H.-J.S.), and Graduate College Grant 612 (to S.B.). | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | BIOMACROMOLECULES | |
dc.subject | CODES | |
dc.subject | EXPRESSION | |
dc.subject | GENE | |
dc.subject | GTP-BINDING PROTEIN | |
dc.subject | INSIGHTS | |
dc.subject | MTO1 | |
dc.subject | MUTANTS | |
dc.subject | POSITION | |
dc.title | Stabilization of G Domain Conformations in the tRNA-modifying MnmE-GidA Complex Observed with Double Electron Electron Resonance Spectroscopy | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M109.096131 | |
dc.identifier.isi | ISI:000277982600062 | |
dc.description.volume | 285 | |
dc.description.issue | 22 | |
dc.description.startpage | 16991 | |
dc.description.endpage | 17000 | |
dc.contributor.orcid | 0000-0002-5761-5968 | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.researcherid | C-1428-2009 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.identifier.eissn | 1083351X | |
dc.publisher.place | 11200 ROCKVILLE PIKE, SUITE 302, ROCKVILLE, MD, UNITED STATES | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | Green Published, hybrid | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
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geprüft am 06.06.2024