Highly efficient over-production in E. coli of YvcC, a multidrug-like ATP-binding cassette transporter from Bacillus subtilis

Biochim Biophys Acta. 2002 Sep 20;1565(1):1-5. doi: 10.1016/s0005-2736(02)00515-1.

Abstract

ATP-binding cassette (ABC) transporters have often been refractory to over-expression. Using the C41(DE3) E. coli as a host strain, membrane vesicles highly enriched (>50%) in YvcC, a previously uncharacterized ABC transporter from Bacillus subtilis homologous to P-glycoprotein multidrug transporters, were obtained. The functionality of YvcC was assessed by its high vanadate-sensitive ATPase activity and its ability to transport a fluorescent drug, the Hoechst 33342.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 1 / biosynthesis
  • ATP-Binding Cassette Transporters / biosynthesis*
  • Bacillus subtilis / genetics*
  • Bacterial Outer Membrane Proteins / biosynthesis*
  • Benzimidazoles / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Fluorescent Dyes / metabolism
  • Vanadates

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 1
  • ATP-Binding Cassette Transporters
  • Bacterial Outer Membrane Proteins
  • Benzimidazoles
  • Fluorescent Dyes
  • Vanadates
  • bisbenzimide ethoxide trihydrochloride