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Article

A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America - 1 Apr 2003

Geissler Brett, Elraheb Dany, Margolin William

Abstract excerpt

ZipA and FtsA are recruited independently to the FtsZ cytokinetic ring (Z ring) and are essential for cell division of Escherichia coli. The molecular role of FtsA in cell division is unknown; however, ZipA is thought to stabilize the Z ring, anchor it to the membrane, and recruit downstream cell division proteins. Here we demonstrate that the requirement for ZipA can be bypassed completely by a single alteration...

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Identifiers

PMID: 12634424
DOI: 10.1073/pnas.0635003100
PMCID: PMC153070

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A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli.PMID 12634424Read ↗

Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.Semantic proximity Read ↗

The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring.Semantic proximity Read ↗

Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli.Semantic proximity Read ↗

A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling.Semantic proximity Read ↗

Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Semantic proximity Read ↗

An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli.Semantic proximity Read ↗

A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.Semantic proximity Read ↗

ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.Semantic proximity Read ↗

Identification of a region of FtsA required for interaction with FtsZ.Semantic proximity Read ↗

Suppression of a Thermosensitive zipA Cell Division Mutant by Altering Amino Acid Metabolism.Semantic proximity Read ↗

The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring.Semantic proximity Read ↗

ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.Semantic proximity Read ↗

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