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

Emmanuelle Steinfels; Cédric Orelle; Olivier Dalmas; François Penin; Bruno Miroux; Attilio Di Pietro; Jean-Michel Jault

doi:10.1016/s0005-2736(02)00515-1

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.

Authors

Emmanuelle Steinfels¹, Cédric Orelle, Olivier Dalmas, François Penin, Bruno Miroux, Attilio Di Pietro, Jean-Michel Jault

Affiliation

¹ Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université Claude Bernard Lyon I, 7 passage du Vercors, 69367, Lyon, France. [email protected]

PMID: 12225846
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