Open AccessThe hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC+
Author(s) -
Cristina Ortiz,
Mercedes Casanova,
Pilar Palacios,
Miguel Vicente
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0184184
Subject(s) - ftsz , mutant , overproduction , escherichia coli , cell division , microbiology and biotechnology , cytoplasm , biology , wild type , chemistry , biochemistry , biophysics , cell , gene
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 + . An excess of FtsA + 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.