Unknown

Dataset Information

0

Dispersion by Pseudomonas aeruginosa requires an unusual posttranslational modification of BdlA.


ABSTRACT: Dispersion enables biofilm bacteria to transit from the biofilm to the planktonic growth state and to spawn novel communities in new locales. Although the chemotaxis protein BdlA plays a role in the dispersion of Pseudomonas aeruginosa biofilms in response to environmental cues, little is known about regulation of BdlA activity or how BdlA modulates the dispersion response. Here, we demonstrate that BdlA in its native form is inactive and is activated upon nonprocessive proteolysis at a ClpP-protease-like cleavage site located between the Per Arnt Sim (PAS) sensory domains PASa and PASb. Activation of BdlA to enable biofilm dispersion requires phosphorylation at tyrosine-238 as a signal, elevated c-di-GMP levels, the chaperone ClpD, and the protease ClpP. The resulting truncated BdlA polypeptide chains directly interact and are required for P. aeruginosa biofilms to disperse. Our results provide a basis for understanding the mechanism of biofilm dispersion that may be applicable to a large number of biofilm-forming pathogenic species. Insights into the mechanism of BdlA function have implications for the control of biofilm-related infections.

SUBMITTER: Petrova OE 

PROVIDER: S-EPMC3478618 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Dispersion by Pseudomonas aeruginosa requires an unusual posttranslational modification of BdlA.

Petrova Olga E OE   Sauer Karin K  

Proceedings of the National Academy of Sciences of the United States of America 20120924 41


Dispersion enables biofilm bacteria to transit from the biofilm to the planktonic growth state and to spawn novel communities in new locales. Although the chemotaxis protein BdlA plays a role in the dispersion of Pseudomonas aeruginosa biofilms in response to environmental cues, little is known about regulation of BdlA activity or how BdlA modulates the dispersion response. Here, we demonstrate that BdlA in its native form is inactive and is activated upon nonprocessive proteolysis at a ClpP-pro  ...[more]

Similar Datasets

| S-EPMC2976224 | biostudies-literature
| S-EPMC4068469 | biostudies-literature
| S-EPMC6258049 | biostudies-literature
| S-EPMC523207 | biostudies-literature
| S-EPMC3370607 | biostudies-literature
2014-06-12 | E-GEOD-58390 | biostudies-arrayexpress
| S-EPMC4201860 | biostudies-literature
2014-06-12 | GSE58390 | GEO
| S-EPMC4436075 | biostudies-literature
| S-EPMC4227967 | biostudies-literature