The mechanism for polar localization of the type IVa pilus machine in <i>Myxococcus xanthus</i>.

ABSTRACT:

Importance

Type IVa pili (T4aP) are widespread bacterial cell surface structures with important functions in motility, surface adhesion, biofilm formation, and virulence. Different bacteria have adapted different piliation patterns. To address how these patterns are established, we focused on the bipolar localization of the T4aP machine in the model organism Myxococcus xanthus by studying the localization of the PilQ secretin, the first component of this machine that assembles at the poles. Based on experiments using a combination of fluorescence microscopy, biochemistry, and computational structural analysis, we propose that PilQ, and specifically its AMIN domains, binds septal and polar peptidoglycan, thereby enabling polar Tgl localization, which then stimulates PilQ mult

SUBMITTER: Herfurth M 

PROVIDER: S-EPMC10653833 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature