Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity.

ABSTRACT:

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WspR is a hybrid response regulator-diguanylate cyclase that is phosphorylated by the Wsp signal transduction complex in response to growth of Pseudomonas aeruginosa on surfaces. Active WspR produces cyclic di-GMP (c-di-GMP), which in turn stimulates biofilm formation. In previous work, we found that when activated by phosphorylation, yellow fluorescent protein (YFP)-tagged WspR forms clusters that are visible in individual cells by fluorescence microscopy. Unphosphorylated WspR is diffuse in cells and not visible. Thus, cluster formation is an assay for WspR signal transduction. To understand how and why WspR forms subcellular clusters, we analyzed cluster formation and the enzymatic activities of six single amino acid variants of WspR. In general, increased cluster for

SUBMITTER: Huangyutitham V 

PROVIDER: S-EPMC3663191 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature