Phenotypic convergence mediated by GGDEF-domain-containing proteins

J Bacteriol. 2005 Oct;187(19):6816-23. doi: 10.1128/JB.187.19.6816-6823.2005.

Abstract

GGDEF domain-containing proteins have been implicated in bacterial signal transduction and synthesis of the second messenger molecule cyclic-di-GMP. A number of GGDEF proteins are involved in controlling the formation of extracellular matrices. AdrA (Salmonella enterica serovar Typhimurium) and HmsT (Yersinia pestis) contain GGDEF domains and are required for extracellular cellulose production and biofilm formation, respectively. Here we show that hmsT is able to restore cellulose synthesis to a Salmonella serovar Typhimurium adrA mutant and that adrA can replace hmsT in Y. pestis Hms-dependent biofilm formation. Like Y. pestis HmsT overproducers, Y. pestis cells carrying adrA under the control of an arabinose-inducible promoter produced substantial biofilms in the presence of arabinose. Finally, we demonstrate that HmsT is involved in the synthesis of cyclic di-GMP.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Biofilms
  • Cyclic GMP / analogs & derivatives
  • Cyclic GMP / metabolism
  • Genetic Complementation Test
  • Phenotype
  • Plasmids
  • Protein Structure, Tertiary
  • Salmonella typhimurium / genetics*
  • Salmonella typhimurium / metabolism
  • Signal Transduction / physiology*
  • Yersinia pestis / genetics*
  • Yersinia pestis / metabolism

Substances

  • Bacterial Proteins
  • HMST protein, Yersinia pestis
  • bis(3',5')-cyclic diguanylic acid
  • Cyclic GMP