Regulation of phenolic catabolism in Rhizobium leguminosarum biovar trifolii

J Bacteriol. 1991 Sep;173(17):5546-50. doi: 10.1128/jb.173.17.5546-5550.1991.

Abstract

In members of the family Rhizobiaceae, many phenolic compounds are degraded by the protocatechuate branch of the beta-ketoadipate pathway. In this paper we describe a novel pattern of induction of protocatechuate (pca) genes in Rhizobium leguminosarum biovar trifolii. Isolation of pca mutant strains revealed that 4-hydroxybenzoate, quinate, and 4-coumarate are degraded via the protocatechuate pathway. At least three inducers govern catabolism of 4-hydroxybenzoate to succinyl coenzyme A and acetyl coenzyme A. The enzyme that catalyzes the initial step is induced by its substrate, whereas the catabolite beta-carboxy-cis,cis-muconate induces enzymes for the upper protocatechuate pathway, and beta-ketoadipate elicits expression of the enzyme for a subsequent step, beta-ketoadipate succinyl-coenzyme A transferase. Elucidation of the induction pattern relied in part on complementation of mutant Rhizobium strains by known subclones of Acinetobacter genes expressed off the lac promoter in a broad-host-range vector.

Publication types

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

MeSH terms

  • Acetyl Coenzyme A / biosynthesis
  • Acetyl Coenzyme A / metabolism
  • Acyl Coenzyme A / biosynthesis
  • Acyl Coenzyme A / metabolism
  • Adipates / metabolism
  • Hydroxybenzoates / metabolism
  • Mutation
  • Parabens / metabolism
  • Phenols / metabolism*
  • Plasmids
  • Restriction Mapping
  • Rhizobium / metabolism*

Substances

  • Acyl Coenzyme A
  • Adipates
  • Hydroxybenzoates
  • Parabens
  • Phenols
  • 3-oxoadipic acid
  • protocatechuic acid
  • Acetyl Coenzyme A
  • succinyl-coenzyme A
  • 4-hydroxybenzoic acid