Format

Send to

Choose Destination
J Biol Chem. 2015 Oct 9;290(41):25081-9. doi: 10.1074/jbc.M115.650077. Epub 2015 Sep 1.

The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.

Author information

1
From the Servicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, 28046 Madrid, Spain, Biomol-Informatics S.L., Universidad Autónoma, 28049 Madrid, Spain, esalvarelli@gmail.com.
2
the Centro Nacional de Biotecnología and.
3
the Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, 28040 Madrid, Spain.
4
From the Servicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, 28046 Madrid, Spain.
5
Biomol-Informatics S.L., Universidad Autónoma, 28049 Madrid, Spain, the Molecular Modelling Group, Centro de Biología Molecular "Severo Ochoa," Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain, and.

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.

KEYWORDS:

GTPase; Streptococcus; bacterial division; protein assembly; protein chemistry; protein dynamic

PMID:
26330552
PMCID:
PMC4599012
DOI:
10.1074/jbc.M115.650077
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center