Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ

被引：13

作者：

Salvarelli, Estefania ^{[1
]}

Krupka, Marcin ^{[2
]}

Rivas, German ^{[3
]}

Vicente, Miguel ^{[2
]}

Mingorance, Jesus ^{[1
]}

机构：

[1] Hosp Univ La Paz, IdiPAZ, Microbiol Serv, Madrid 28046, Spain

[2] Ctr Nacl Biotecnol CNB CSIC, Madrid 28049, Spain

[3] Ctr Invest Biol CIB CSIC, Madrid 28040, Spain

来源：

FEBS LETTERS | 2011年 / 585卷 / 24期

关键词：

FtsZ; Cell division; GTPase activity; Escherichia coli; FILAMENT DYNAMICS; HYDROLYSIS; POLYMERIZATION; ACTIVATION; MONOMER; ASSAY;

D O I：

10.1016/j.febslet.2011.10.046

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have analyzed the substrate kinetics of the GTPase activity of FtsZ and the effects of two different GTPase inhibitors, GDP and the slowly hydrolyzable GTP analogue GMPCPP. In the absence of inhibitors the GTPase activity follows simple Michaelis-Menten kinetics, and both GDP and GMPCPP inhibited the activity in a competitive manner. These results indicate that the GTPase active sites in FtsZ filaments are independent of each other, a feature relevant to elucidate the role of GTP hydrolysis in FtsZ function and cell division. Structured summary of protein interactions: FtsZ and FtsZ bind by light scattering (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3880 / 3883

页数：4

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