PMID:12934015
| Citation |
Ermolova, N, Guan, L and Kaback, HR (2003) Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 100:10187-92 |
|---|---|
| Abstract |
Previous experiments using intermolecular thiol cross-linking to determine surface-exposed positions in the transmembrane helices of the lactose permease suggest that only positions accessible from the aqueous phase are susceptible to cross-linking. This approach is now extended to most of the remaining positions in the molecule. Of an additional 143 single-Cys mutants studied, homodimer formation is observed with both a 5-A- and a 21-A-long crosslinking agent containing bis-methane thiosulfonate reactive groups in 33 mutants and exclusively with the 21-A-long reagent in 43 mutants. Furthermore, intermolecular cross-linking has little or no effect on transport activity, thereby providing further support for the argument that lactose permease is functionally, as well as structurally, a monomer in the membrane. In addition, evidence is presented indicating that reentrance loops are unlikely in this polytopic membrane transport protein. |
| Links |
PubMed PMC193537 Online version:10.1073/pnas.1434239100 |
| Keywords |
Amino Acid Sequence; Biological Transport; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Lactose/metabolism; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/physiology; Molecular Sequence Data; Monosaccharide Transport Proteins; Sulfhydryl Compounds/chemistry; Symporters |
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