Regulation of biofilm formation in Yersinia pestis.
Plague biofilm development is controlled by positive (HmsT) and negative (HmsP) regulators. The GGDEF-domain protein HmsT appears to have diguanylate cyclase activity to synthesize bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP) from 2 GTP molecules. The EAL domain of HmsP has phosphodiesterase activity and likely degrades c-di-GMP. This second messenger molecule probably influences biofilm development by activating the glycosyl transferase activity of HmsR. Here we demonstrate the in vitro pH optimum for phosphodiesterase activity of HmsP and that an alanine substitution in residue L508, D626, or E686 within the EAL domain affects this enzymatic activity and the biological function of the protein. Finally, protein-protein interactions and the cytoplasmic location of the enzymatic domains of HmsT and HmsP are evaluated.
Bobrov
Alexander G
AG
Department of Microbiology, Immunology and Molecular Genetics, University of Kentucky, Lexington, USA. bobrov@uky.edu
Kirillina
Olga
O
Perry
Robert D
RD
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D018441:Biofilms / Q000254:growth & development*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006801:Humans; D007303:Insect Vectors / Q000382:microbiology; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D010930:Plague / Q000382:microbiology / Q000635:transmission; D054730:Protein Interaction Domains and Motifs; D005423:Siphonaptera / Q000382:microbiology; D014774:Virulence / Q000235:genetics; D015010:Yersinia pestis / Q000235:genetics / Q000472:pathogenicity / Q000502:physiology*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C122178:HMST protein, Yersinia pestis; D010727:Phosphoric Diester Hydrolases; D019761:Phosphorus-Oxygen Lyases; C060720:diguanylate cyclase