Unknown

Dataset Information

0

The hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.


ABSTRACT: 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.

SUBMITTER: Ortiz C 

PROVIDER: S-EPMC5587298 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

altmetric image

Publications

The hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.

Ortiz Cristina C   Casanova Mercedes M   Palacios Pilar P   Vicente Miguel M  

PloS one 20170906 9


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  ...[more]

Similar Datasets

| S-EPMC3064179 | biostudies-literature
| S-EPMC4686002 | biostudies-literature
| S-EPMC3067613 | biostudies-literature
| S-EPMC5796856 | biostudies-literature
| S-EPMC4732229 | biostudies-literature
| S-EPMC5772807 | biostudies-literature
| S-EPMC8897712 | biostudies-literature
| S-EPMC9879108 | biostudies-literature
| S-EPMC6055203 | biostudies-literature
| S-EPMC5508204 | biostudies-literature