TmrB protein, which confers resistance to tunicamycin on Bacillus subtilis, binds tunicamycin

Biosci Biotechnol Biochem. 1995 Feb;59(2):321-2. doi: 10.1271/bbb.59.321.

Abstract

Overproduction of TmrB protein, a 22.5-kDa protein with an N-terminal ATP-binding region and a C-terminal amphiphilic alpha-helix, confers resistance to tunicamycin on Bacillus subtilis. TmrB protein was found to bind Sepharose 6B to which tunicamycin was covalently linked. Experiments with mutant proteins found that the C-terminal region of TmrB protein might be involved in the binding to tunicamycin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Binding, Competitive
  • Blotting, Western
  • Chemical Fractionation
  • Drug Resistance, Microbial
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression Regulation, Bacterial / genetics
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Weight
  • Mutation
  • Precipitin Tests
  • Tunicamycin / metabolism*

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Tunicamycin
  • tmrB protein, Bacillus subtilis