Evidence that the NH2 terminus of Vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 15449-15457

  Landolt Marticorena, Carolina ^a,c   Williams, Kelly M ^b   Correa, Judy ^a   Chen, Weimin ^a   Manolson, Morris F ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; TRYPSIN; PEPTIDE FRAGMENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBUNIT; HYDROLYSIS; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ACTIVITY RELATION; CELL VACUOLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; INTRACELLULAR MEMBRANE; KINETICS; MACROMOLECULE; METABOLISM; PLASMID; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; THERMODYNAMICS; TORQUE;

ESCHERICHIA COLI; INTRACELLULAR MEMBRANES; KINETICS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PLASMIDS; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; THERMODYNAMICS; TORQUE; VACUOLAR PROTON-TRANSLOCATING ATPASES; VACUOLES;

EID: 0034685544     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M000207200     Document Type: Article

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