A Cyclic-di-GMP Receptor Required for Bacterial Exopolysaccharide Production

DSpace/Manakin Repository

A Cyclic-di-GMP Receptor Required for Bacterial Exopolysaccharide Production

Citable link to this page

. . . . . .

Title: A Cyclic-di-GMP Receptor Required for Bacterial Exopolysaccharide Production
Author: Matewish, Jody M; Kessler, Jennifer L; Hyodo, Mamoru; Hayakawa, Yoshihiro; Lee, Vincent T.; Lory, Stephen

Note: Order does not necessarily reflect citation order of authors.

Citation: Lee, Vincent T., Jody M. Matewish, Jennifer L. Kessler, Mamoru Hyodo, Yoshihiro Hayakawa, and Stephen Lory. 2007. A cyclic-di-GMP receptor required for bacterial exopolysaccharide production. Molecular Microbiology 65(6): 1474-1484.
Full Text & Related Files:
Abstract: Bis-(3′,5′)-cyclic-dimeric-guanosine monophosphate (c-di-GMP) has been shown to be a global regulatory molecule that modulates the reciprocal responses of bacteria to activate either virulence pathways or biofilm formation. The mechanism of c-di-GMP signal transduction, including recognition of c-di-GMP and subsequent phenotypic regulation, remain largely uncharacterized. The key components of these regulatory pathways are the various adaptor proteins (c-di-GMP receptors). There is compelling evidence suggesting that, in addition to PilZ domains, there are other unidentified c-di-GMP receptors. Here we show that the PelD protein of Pseudomonas aeruginosa is a novel c-di-GMP receptor that mediates c-di-GMP regulation of PEL polysaccharide biosynthesis. Analysis of PelD orthologues identified a number of conserved residues that are required for c-di-GMP binding as well as synthesis of the PEL polysaccharide. Secondary structure similarities of PelD to the inhibitory site of diguanylate cyclase suggest that a common fold can act as a platform to bind c-di-GMP. The combination of a c-di-GMP binding site with a variety of output signalling motifs within one protein domain provides an explanation for the specificity for different cellular responses to this regulatory dinucleotide.d
Published Version: doi:10.1111/j.1365-2958.2007.05879.x
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2170427/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4632771

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters