The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

被引:20
作者
Conti, Joseph [1 ]
Viola, Marissa G. [1 ]
Camberg, Jodi L. [1 ,2 ]
机构
[1] Univ Rhode Isl, Dept Cell & Mol Biol, Kingston, RI 02881 USA
[2] Univ Rhode Isl, Dept Nutr & Food Sci, Kingston, RI 02881 USA
关键词
MinE; ATPase; Phospholipids; Cytokinesis; Min system; ESCHERICHIA-COLI; MEMBRANE-BINDING; DNA-SEGREGATION; INHIBITOR MINC; SITE SELECTION; C-TERMINUS; IN-VITRO; Z-RING; FTSZ; ATPASE;
D O I
10.1016/j.febslet.2014.11.047
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
The Min system of proteins, consisting of MinC, MinD and MinE, is essential for normal cell division in Escherichia coli. MinC forms a polar gradient to restrict placement of the division septum to midcell. MinC localization occurs through a direct interaction with MinD, a membrane-associating Par-like ATPase. MinE stimulates ATP hydrolysis by MinD, thereby releasing MinD from the membrane. Here, we show that MinD forms polymers with MinC and ATP without the addition of phospholipids. The topological regulator MinE induces disassembly of MinCD polymers. Two MinD mutant proteins, MinD(K11A) and MinD(DMTS15), are unable to form polymers with MinC. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:201 / 206
页数:6
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