Thioesterases and the premature termination of polyketide chain elongation in rifamycin B biosynthesis by Amycolatopsis mediterranei S699

J Antibiot (Tokyo). 2000 May;53(5):484-95. doi: 10.7164/antibiotics.53.484.

Abstract

The role of two thioesterase genes in the premature release of polyketide synthase intermediates during rifamycin biosynthesis in the Amycolatopsis mediterranei S699 strain was investigated. Creation of an in-frame deletion in the rifR gene led to a 30 approximately 60% decrease in the production of both rifamycin B by the S699 strain or a series of tetra- to decaketide shunt products of polyketide chain assembly by the rifF strain. Since a similar percentage decrease was seen in both genetic backgrounds, we conclude that the RifR thioesterase 2 is not involved in premature release of the carbon chain assembly intermediates. Similarly, fusion of the Saccharopolyspora erythraea DEBS3 thioesterase I domain to the C-terminus of the RifE PKS subunit did not result in a noticeable increase in the amount of the undecaketide intermediate formed nor in the amounts of the tetra- to decaketide shunt products. Hence, premature release of the carbon chain assembly intermediates is an unusual property of the Rif PKS itself.

Publication types

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

MeSH terms

  • Actinomycetales / genetics
  • Actinomycetales / metabolism*
  • Amino Acid Sequence
  • Anti-Bacterial Agents / biosynthesis*
  • Base Sequence
  • Esterases / metabolism*
  • Genes, Bacterial
  • Molecular Sequence Data
  • Multienzyme Complexes / genetics
  • Mutation
  • Peptide Chain Elongation, Translational*
  • Rifamycins / biosynthesis*

Substances

  • Anti-Bacterial Agents
  • Multienzyme Complexes
  • Rifamycins
  • rifamycin B
  • Esterases