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The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide
Author(s) -
Conti Joseph,
Viola Marissa G.,
Camberg Jodi L.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.047
Subject(s) - cell division , regulator , microbiology and biotechnology , chemistry , polymer , cell , atpase , mutant , biophysics , biology , biochemistry , gene , enzyme , organic chemistry
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(ΔMTS 15 ), are unable to form polymers with MinC.