Affiliation:
1. Department of Biology, University of Texas at Arlington, Arlington, Texas 76019
Abstract
ABSTRACT
The membrane topology of the ZntB Zn
2+
transport protein of
Salmonella enterica
serovar Typhimurium was determined by constructing deletion derivatives of the protein and genetically fusing them to
blaM
or
lacZ
cassettes. The enzymatic activities of the hybrid proteins indicate that ZntB is a bitopic integral membrane protein consisting largely of two independent domains. The first 266 amino acids form a large, highly charged domain within the cytoplasm, while the remaining 61 residues form a small membrane domain containing two membrane-spanning segments. The overall orientation towards the cytoplasm is consistent with the ability of ZntB to facilitate zinc efflux.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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