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

Abstract:

:The cytokinetic apparatus of bacteria is initially formed by the polymerization of the tubulin-like FtsZ protein into a ring structure at midcell. This so-called Z-ring facilitates the recruitment of many additional proteins to the division site to form the mature divisome machine. Although the assembly pathway leading to divisome formation has been well characterized, the mechanisms that trigger cell constriction remain unclear. In this report, we study a 'forgotten' allele of ftsL from Escherichia coli, which encodes a conserved division gene of unknown function. We discovered that this allele promotes the premature initiation of cell division. Further analysis also revealed that the mutant bypasses the requirement for the essential division proteins ZipA, FtsK and FtsN, and partially bypasses the need for FtsA. These findings suggest that rather than serving simply as a protein scaffold within the divisome, FtsL may play a more active role in the activation of the machine. Our results support a model in which FtsL, along with its partners FtsB and FtsQ, function as part of a sensing mechanism that promotes the onset of cell wall remodeling processes needed for the initiation of cell constriction once assembly of the divisome complex is deemed complete.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Tsang MJ,Bernhardt TG

doi

10.1111/mmi.12905

subject

Has Abstract

pub_date

2015-03-01 00:00:00

pages

925-44

issue

6

eissn

0950-382X

issn

1365-2958

journal_volume

95

pub_type

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