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The hypermorph FtsA protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.sup.
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The hypermorph FtsA protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.sup.
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The hypermorph FtsA protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.sup.
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Journal Article
The hypermorph FtsA protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.sup.
2017
Overview
Assembly of the proto-ring, formed by the essential FtsZ, FtsA and ZipA proteins, and its progression into a divisome, are essential events for Escherichia coli division. ZapC is a cytoplasmic protein that belongs to a group of non-essential components that assist FtsZ during proto-ring assembly. Any overproduction of these proteins leads to faulty FtsZ-rings, resulting in a cell division block. We show that ZapC overproduction can be counteracted by an excess of the ZipA-independent hypermorph FtsA* mutant, but not by similar amounts of wild type FtsA.sup.+ . An excess of FtsA.sup.+ allowed regular spacing of the ZapC-blocked FtsZ-rings, but failed to promote recruitment of the late-assembling proteins FtsQ, FtsK and FtsN and therefore, to activate constriction. In contrast, overproduction of FtsA*, besides allowing correct FtsZ-ring localization at midcell, restored the ability of FtsQ, FtsK and FtsN to be incorporated into active divisomes.
Publisher
Public Library of Science
Subject
