Roles of LuxR in regulating extracellular alkaline serine protease A, extracellular polysaccharide and mobility of Vibrio alginolyticus

FEMS Microbiol Lett. 2008 Aug;285(2):155-62. doi: 10.1111/j.1574-6968.2008.01185.x. Epub 2008 Jun 28.

Abstract

In marine Vibrio species, the Vibrio harveyi-type LuxR protein, a key player in a quorum-sensing system, controls the expression of various genes. In this study, the luxR homologue in Vibrio alginolyticus was identified and named luxR(val), whose expression was greatly induced by the increase of cell number. The luxR(val) in-frame deletion mutant showed a significant downregulation of total extracellular protease activity, and especially caused a 70% decrease in the transcript levels of extracellular alkaline serine protease A (proA), which was an important virulent factor of V. alginolyticus. Complementation in trans with luxR(val) could restore the expression of proA to the level of the wild-type strain. Deletion of the luxR(val) gene also resulted in changes of colony morphology, extracellular polysaccharide production and mobility. Therefore, another member of the V. harveyi-type LuxR regulator family has been characterized in V. alginolyticus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / biosynthesis*
  • Gene Deletion
  • Gene Expression Profiling
  • Genetic Complementation Test
  • Locomotion*
  • Polysaccharides, Bacterial / biosynthesis*
  • RNA, Bacterial / biosynthesis
  • RNA, Messenger / biosynthesis
  • Repressor Proteins / genetics
  • Repressor Proteins / physiology*
  • Serine Endopeptidases / biosynthesis*
  • Trans-Activators / genetics
  • Trans-Activators / physiology*
  • Vibrio alginolyticus / enzymology*
  • Vibrio alginolyticus / genetics
  • Vibrio alginolyticus / physiology*

Substances

  • Bacterial Proteins
  • Polysaccharides, Bacterial
  • RNA, Bacterial
  • RNA, Messenger
  • Repressor Proteins
  • Trans-Activators
  • LuxR autoinducer binding proteins
  • Serine Endopeptidases