VANADATE AND BAFILOMYCIN A(1) ARE POTENT INHIBITORS OF THE ATPASE ACTIVITY OF THE RECONSTITUTED BACTERIAL ATP-BINDING CASSETTE TRANSPORTER FOR MALTOSE (MALFGK(2))

Autor(en): HUNKE, S 
DROSE, S
SCHNEIDER, E 
Stichwörter: ADENYLATE KINASE; Biochemistry & Molecular Biology; Biophysics; COMPLEX; ESCHERICHIA-COLI; H+-ATPASE; MALK SUBUNIT; NUCLEOTIDE-BINDING; PROTEINS; PURIFICATION; SALMONELLA-TYPHIMURIUM; TRANSLOCATING KDP-ATPASE
Erscheinungsdatum: 1995
Herausgeber: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS
Journal: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volumen: 216
Ausgabe: 2
Startseite: 589
Seitenende: 594
Zusammenfassung: 
Vanadate and Bafilomycin A(1) were shown to inhibit the ATPase activity of the reconstituted binding protein-dependent ATP-Binding Cassette (ABC) transporter for maltose (MalFGK(2)) of Salmonella typhimurium in the micromolar range. This is in sharp contrast to the recent finding that the isolated ATPase subunit MalK was insensitive to both compounds. Our data provide the first experimental evidence for the view that functional coupling of the ATPase domain of an ABC transporter to the membrane-integral domains is crucial for conferring sensitivity to vanadate and bafilomycin A(1). Possible consequences for the mode of action of ABC transport proteins are discussed. (C) 1995 Academic Press, Inc.
ISSN: 0006291X
DOI: 10.1006/bbrc.1995.2663

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