Bypassing the need for subcellular localization of a polysaccharide export-anchor complex by overexpressing its protein subunits.

ABSTRACT: Subcellular protein localization is thought to promote protein-protein interaction by increasing the effective concentration and enabling spatial co-ordination and proper segregation of proteins. We found that protein overexpression allowed the assembly of a productive polysaccharide biosynthesis-export-anchoring complex in the absence of polar localization in Caulobacter crescentus. Polar localization of the holdfast export protein, HfsD, depends on the presence of the other export proteins, HfsA and HfsB, and on the polar scaffold protein PodJ. The holdfast deficiency of hfsB and podJ mutants is suppressed by the overexpression of export proteins. Restored holdfasts are randomly positioned and colocalize with a holdfast anchor protein in these strains, indicating that functional complexe

SUBMITTER: Javens J 

PROVIDER: S-EPMC3740972 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature