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dc.contributor.author | Salvarelli, Estefanía | - |
dc.contributor.author | Krupka, Marcin | - |
dc.contributor.author | Rivas, Germán | - |
dc.contributor.author | Mingnorance, Jesús | - |
dc.contributor.author | Gómez-Puertas, Paulino | - |
dc.contributor.author | Alfonso, Carlos | - |
dc.contributor.author | Rico, Ana Isabel | - |
dc.date.accessioned | 2016-11-22T09:58:31Z | - |
dc.date.available | 2016-11-22T09:58:31Z | - |
dc.date.issued | 2015-09-01 | - |
dc.identifier | doi: 10.1074/jbc.M115.650077 | - |
dc.identifier | issn: 1083-351X | - |
dc.identifier.citation | Journal of Biological Chemistry 290: 25081- 25089 (2015) | - |
dc.identifier.uri | http://hdl.handle.net/10261/140539 | - |
dc.description.abstract | © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.. The cell division protein FtsZ assembles in vitro by a mechanism of cooperative association dependent on GTP, monovalent cations, and Mg2+. We have analyzed the GTPase activity and assembly dynamics of Streptococcus pneumoniae FtsZ (Spn-FtsZ). SpnFtsZ assembled in an apparently cooperative process, with a higher critical concentration than values reported for other FtsZ proteins. It sedimented in the presence of GTP as a high molecular mass polymer with a well defined size and tended to form double-stranded filaments in electron microscope preparations. GTPase activity depended on K+ and Mg2+ and was inhibited by Na+. GTP hydrolysis exhibited a delay that included a lag phase followed by a GTP hydrolysis activation step, until reaction reached the GTPase rate. The lag phase was not found in polymer assembly, suggesting a transition from an initial non-GTP-hydrolyzing polymer that switches to a GTP-hydrolyzing polymer, supporting models that explain FtsZ polymer cooperativity. | - |
dc.description.sponsorship | Spanish Government GrantsBIO2011-28941-C03 (to G. R. and C. A.) and BIO2011-28941-C01; Torres Quevedo Program Grant PTQ-11-05049 to Biomol Informatics S.L. | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation.isversionof | Publisher's version | - |
dc.rights | openAccess | - |
dc.title | The cell division protein FtsZ from Streptococcus pneumoniae exhibits a GTPase activity delay | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1074/jbc.M115.650077 | - |
dc.date.updated | 2016-11-22T09:58:32Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.contributor.funder | Fundación Leonardo Torres Quevedo | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.pmid | 26330552 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
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Gomez-Puertas P The cell division.pdf | 1,86 MB | Adobe PDF | Visualizar/Abrir |
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