Open AccessTopological studies of the membrane component of the OleC ABC transporter involved in oleandomycin resistance in Streptomyces antibioticus
Author(s) -
Olano Carlos,
Rodriguez Ana Maria,
Méndez Carmen,
Salas JoséA.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08472.x
Subject(s) - periplasmic space , atp binding cassette transporter , transmembrane domain , transmembrane protein , integral membrane protein , membrane transport protein , biology , biochemistry , oleandomycin , membrane protein , streptomyces , escherichia coli , cloning (programming) , topology (electrical circuits) , chemistry , gene , transporter , membrane , genetics , bacteria , receptor , mathematics , combinatorics , erythromycin , computer science , programming language , antibiotics
The OleC ABC transporter of Streptomyces antibioticus is constituted by an ATP‐binding protein (OleC) and a Hydrophobic protein (OleCS). Here we present experimental evidence demonstrating that the OleCS protein is an integral membrane protein and we propose a topological model for its integration into the membrane. This model is based on the generation of hybrid proteins between different regions of OleCS and a Escherichia coli β‐lactamase (BlaM) and the determination of the minimal inhibitory concentrations to ampicillin in these constructions. Fusions were generated both by cloning specific fragments of oleC5 and by creating Exo III nested deletions of the gene. In the topological model proposed there will be six a‐helix transmembrane regions, two cytoplasmic and four periplasmic loops and a hydrophobic linker domain.