Regulation of hut enzymes and intracellular protease activities in Vibrio alginolyticus hut mutants

J Gen Microbiol. 1982 Sep;128(9):2041-5. doi: 10.1099/00221287-128-9-2041.

Abstract

The production of alkaline protease, collagenase and histidine utilization (Hut) enzymes by Vibrio alginolyticus wild-type, hutH1 and hutU1 strains was investigated. Alkaline protease synthesis was stimulated by histidine and urocanic acid in the wild-type and hutU1 strains. The hutH1 mutant alkaline protease production was stimulated by urocanic acid and not by histidine. The Hut enzymes in the wild-type strain were coordinately induced by histidine. Urocanase and formimino-hydrolase were induced by histidine in the hutH1 mutant which lacked histidase and was not able to convert histidine to urocanic acid. Collagenase production in peptone medium was inhibited in the hut mutants. It is concluded that in V. alginolyticus urocanic acid regulates alkaline protease synthesis but that the Hut enzymes are induced by histidine. The involvement of the Hut genetic system in the regulation of alkaline protease and collagenase synthesis is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Endopeptidases / biosynthesis*
  • Enzyme Induction
  • Histidine / metabolism*
  • Histidine Ammonia-Lyase / biosynthesis
  • Hydrolases / biosynthesis
  • Microbial Collagenase / biosynthesis*
  • Mutation
  • Serine Endopeptidases*
  • Urocanate Hydratase / biosynthesis
  • Vibrio / enzymology*
  • Vibrio / genetics

Substances

  • Bacterial Proteins
  • Histidine
  • Hydrolases
  • Endopeptidases
  • Serine Endopeptidases
  • Vibrio alginolyticus alkaline protease
  • Microbial Collagenase
  • EE57C protein, Bacillus subtilis
  • Urocanate Hydratase
  • Histidine Ammonia-Lyase