Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB.

ABSTRACT: Most bacteria and archaea use the tubulin homologue FtsZ as its central organizer of cell division. In Gram-negative Escherichia coli bacteria, FtsZ recruits cytosolic, transmembrane, periplasmic, and outer membrane proteins, assembling the divisome that facilitates bacterial cell division. One such divisome component, FtsQ, a bitopic membrane protein with a globular domain in the periplasm, has been shown to interact with many other divisome proteins. Despite its otherwise unknown function, it has been shown to be a major divisome interaction hub. Here, we investigated the interactions of FtsQ with FtsB and FtsL, two small bitopic membrane proteins that act immediately downstream of FtsQ. We show in biochemical assays that the periplasmic domains of E. coli FtsB and FtsL int

SUBMITTER: Kureisaite-Ciziene D 

PROVIDER: S-EPMC6134095 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature