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Authordc.contributor.authorNova Martínez, Esteban 
Authordc.contributor.authorMontecinos, Felipe es_CL
Authordc.contributor.authorBrunet, Juan E. es_CL
Authordc.contributor.authorLagos Mónaco, Rosalba es_CL
Authordc.contributor.authorMonasterio Opazo, Octavio es_CL
Admission datedc.date.accessioned2010-03-08T19:02:46Z
Available datedc.date.available2010-03-08T19:02:46Z
Publication datedc.date.issued2007-09-15
Cita de ítemdc.identifier.citationARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, Volume: 465, Issue: 2, Pages: 315-319, 2007en_US
Identifierdc.identifier.issn0003-9861
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/119012
Abstractdc.description.abstractFtsZ (Filamentous temperature sensitivity Z) cell division protein from Escherichia coli binds the fluorescence probe DAPI. Bundling of FtsZ was facilitated in the presence of DAPI, and the polymers in solution remained polymerized longer time than the protofilaments formed in the absence of DAPI. DAPI decreased both the maximal velocity of the GTPase activity and the Michaelis–Menten constant for GTP, indicating that behaves like an uncompetitive inhibitor of the GTPase activity favoring the GTP form of FtsZ in the polymers. The results presented in this work support a cooperative polymerization mechanism in which the binding of DAPI favors protofilament lateral interactions and the stability of the resulting polymers.en_US
Patrocinadordc.description.sponsorshipThis work was supported by Grants 1050677 and 7060162 from FONDECYT (Chile), MECESUP Grant UCH0116 and CSIC/Universidad de Chile, Grant CSIC 03/04-15.en_US
Lenguagedc.language.isoenen_US
Publisherdc.publisherELSEVIER SCIENCE INCen_US
Keywordsdc.subjectEcFtsZen_US
Títulodc.title4',6-Diamidino-2-phenylindole (DAPI) induces bundling of Escherichia coli FtsZ polymers inhibiting the GTPase activityen_US
Document typedc.typeArtículo de revista


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