The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.
J Biol Chem
; 290(41): 25081-9, 2015 Oct 09.
Article
en En
| MEDLINE
| ID: mdl-26330552
ABSTRACT
The cell division protein FtsZ assembles in vitro by a mechanism of cooperative association dependent on GTP, monovalent cations, and Mg(2+). We have analyzed the GTPase activity and assembly dynamics of Streptococcus pneumoniae FtsZ (SpnFtsZ). 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 Mg(2+) 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.
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Banco de datos:
MEDLINE
Asunto principal:
Streptococcus pneumoniae
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Proteínas Bacterianas
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Proteínas del Citoesqueleto
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GTP Fosfohidrolasas
Idioma:
En
Año:
2015
Tipo del documento:
Article