Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP.
Science, 2010/2/12;327(5967):866-8.
Krasteva PV[1], Fong JC, Shikuma NJ, Beyhan S, Navarro MV, Yildiz FH, Sondermann H
Affiliations
PMID: 20150502DOI: 10.1126/science.1181185
Impact factor: 63.714
Abstract
Microorganisms can switch from a planktonic, free-swimming life-style to a sessile, colonial state, called a biofilm, which confers resistance to environmental stress. Conversion between the motile and biofilm life-styles has been attributed to increased levels of the prokaryotic second messenger cyclic di-guanosine monophosphate (c-di-GMP), yet the signaling mechanisms mediating such a global switch are poorly understood. Here we show that the transcriptional regulator VpsT from Vibrio cholerae directly senses c-di-GMP to inversely control extracellular matrix production and motility, which identifies VpsT as a master regulator for biofilm formation. Rather than being regulated by phosphorylation, VpsT undergoes a change in oligomerization on c-di-GMP binding.
MeSH terms
Amino Acid Motifs; Bacterial Proteins; Binding Sites; Biofilms; Crystallography, X-Ray; Cyclic GMP; DNA, Bacterial; Dimerization; Extracellular Matrix; Gene Expression Profiling; Gene Expression Regulation, Bacterial; Models, Molecular; Movement; Point Mutation; Polysaccharides, Bacterial; Protein Folding; Protein Multimerization; Protein Structure, Tertiary; Signal Transduction; Transcription Factors; Transcription, Genetic; Vibrio cholerae O1
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