The Amino-terminal Domain of the Vacuolar Proton-translocating ATPase a Subunit Controls Targeting and in Vivo Dissociation, and the Carboxyl-terminal Domain Affects Coupling of Proton Transport and ATP Hydrolysis

Journal of Biological Chemistry

Volumn 276, Issue 50, 2001, Pages 47411-47420

  Kawasaki Nishi, Shoko ^a   Bowers, Katherine ^b   Nishi, Tsuyoshi ^a   Forgac, Michael ^a   Stevens, Tom H ^b  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; GENES; GLUCOSE; HYDROLYSIS; YEAST;

GOLGI COMPARTMENT;

PROTONS;

ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE TRIPHOSPHATASE; GLUCOSE; HYBRID PROTEIN; ISOPROTEIN; PROTON; VACUOLAR H+ ATPASE; VACUOLAR H+-ATPASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL COMPARTMENTALIZATION; CELL VACUOLE; CHIMERA; COMPLEX FORMATION; CYTOSOL; DISSOCIATION; ENDOSOME; ENZYME ANALYSIS; ENZYME SUBUNIT; FUNGAL GENE; GENE LOCATION; GENE TARGETING; GLUCOSE METABOLISM; GOLGI COMPLEX; HYDROLYSIS; IN VIVO STUDY; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN TARGETING; PROTON TRANSPORT; STEADY STATE; STV1 GENE; VPH1 GENE; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMISTRY; FLUORESCENCE MICROSCOPY; GENE DELETION; GENETICS; METABOLISM; MOLECULAR GENETICS; PLASMID; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SERODIAGNOSIS; WESTERN BLOTTING; YEAST;

ADENOSINE TRIPHOSPHATE; ADENOSINETRIPHOSPHATASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BLOTTING, WESTERN; CELL MEMBRANE; GENE DELETION; GLUCOSE; GOLGI APPARATUS; HYDROLYSIS; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; PLASMIDS; PRECIPITIN TESTS; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; PROTONS; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; VACUOLAR PROTON-TRANSLOCATING ATPASES; VACUOLES; YEASTS;

EID: 0035861664     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M108310200     Document Type: Article

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