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

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• 作者：Estefaní ; a  ; Salvarelli^a ; Marcin  ; Krupka^b ; Germá ; n  ; Rivas^c ; Miguel  ; Vicente^b ; Jesú ; s  ; Mingorance^a ;   ; ^{jesus.mingorance@idipaz.es} ;   ; ^{jmingorancec.hulp@salud.madrid.org}
• 关键词：FtsZ ; Cell division ; GTPase activity ; Escherichia coli
• 刊名：FEBS Letters
• 出版年：2011
• 出版时间：15 December 2011
• 年：2011
• 卷：585
• 期：24
• 页码：3880-3883
• 全文大小：347 K

文摘

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¨CMenten 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

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