A Cyclic-di-GMP Receptor Required for Bacterial Exopolysaccharide Production
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A Cyclic-di-GMP Receptor Required for Bacterial Exopolysaccharide Production
| 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: |
2170427.pdf (1.669Mb; PDF) 
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| 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 |
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