| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10870436 | FEBS Letters | 2015 | 6 Pages |
Abstract
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(ÎMTS15), are unable to form polymers with MinC.
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Authors
Joseph Conti, Marissa G. Viola, Jodi L. Camberg,