Unknown

Dataset Information

0

A 1 MDa protein complex containing critical components of the Escherichia coli divisome.


ABSTRACT: Cell division in bacteria is an essential process that is carried out at mid-cell by a group of cell division proteins referred to as the divisome. In Escherichia coli, over two dozen cell division proteins have been identified of which ten are essential. These division proteins localize sequentially and interdependently to the division site, after which constriction eventually produces two daughter cells. Various genetic and biochemical techniques have identified many interactions amongst cell division proteins, however the existence of the divisome as a large multi-protein complex has never been shown. Here, we identify a 1 MDa protein complex by native page that contains seven essential cell division proteins (FtsZ, ZipA, FtsK, FtsQ, FtsB, FtsL, and FtsN). The 1 MDa complex is present in rapidly dividing cells, but absent when cultures enter the stationary growth phase. Slight overexpression of the ftsQ D237N mutation that blocks cell division prevents formation of this 1 MDa complex. In cells depleted of FtsN, the 1 MDa complex is not assembled. Combined, our findings indicate that a large protein complex containing many different cell division proteins indeed exists. We note that this complex is very fragile and sensitive to the expression of tagged versions of FtsQ.

SUBMITTER: Trip EN 

PROVIDER: S-EPMC4672292 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

A 1 MDa protein complex containing critical components of the Escherichia coli divisome.

Trip Erik N EN   Scheffers Dirk-Jan DJ  

Scientific reports 20151208


Cell division in bacteria is an essential process that is carried out at mid-cell by a group of cell division proteins referred to as the divisome. In Escherichia coli, over two dozen cell division proteins have been identified of which ten are essential. These division proteins localize sequentially and interdependently to the division site, after which constriction eventually produces two daughter cells. Various genetic and biochemical techniques have identified many interactions amongst cell  ...[more]

Similar Datasets

| S-EPMC6904479 | biostudies-literature
| S-EPMC9098913 | biostudies-literature
| S-EPMC8897712 | biostudies-literature
| S-EPMC5404276 | biostudies-literature
| S-EPMC4004784 | biostudies-literature
| S-EPMC6055203 | biostudies-literature
| S-EPMC4462998 | biostudies-literature
| S-EPMC8620860 | biostudies-literature
| S-EPMC4125044 | biostudies-literature
| S-EPMC5996693 | biostudies-literature