Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signaling.
Periplasmic permeases consist of a substrate-binding receptor, located in the periplasm, and a membrane-bound complex composed of two integral membrane proteins and two nucleotide-binding proteins. The receptor interacts with the membrane-bound complex, which, upon receiving this signal, is postulated to hydrolyze ATP and translocate the substrate. We show that a class of mutations in the membrane-bound complex of the histidine permease, which allow transport in the absence of the substrate-binding protein, hydrolyze ATP independently from any signal. The data are compatible with the notion that cross-membrane signaling between the liganded periplasmic receptor and the cytoplasmic ATP-binding sites initiates conformational changes leading to ATP hydrolysis and substrate translocation.[1]References
- Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signaling. Petronilli, V., Ames, G.F. J. Biol. Chem. (1991) [Pubmed]
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