Studies of the interaction of substituted mutants of BAX with yeast mitochondria reveal that the C-terminal hydrophobic α-helix is a second ART sequence and plays a role in the interaction with anti-apoptotic BCL-x L

Journal of Biological Chemistry

Volumn 279, Issue 50, 2004, Pages 52566-52573

  Arokium, Hubert ^a   Camougrand, Nadine ^a   Vallette, François M ^b   Manon, Stéphen ^a  

^a UNIVERSITÉ DE BORDEAUX   (France)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; HYDROPHOBICITY; MUTAGENS; PROTEINS; SUBSTITUTION REACTIONS;

APOPTOTIC REGULATION OF TARGETING (ART); CYTOCHROMES; MITOCHONDRIA; MUTATIONS;

YEAST;

BINDING PROTEIN; CYTOCHROME C; MUTANT PROTEIN; PROTEIN BAX; PROTEIN BCL XL;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; MITOCHONDRIAL MEMBRANE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; YEAST CELL;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; APOPTOSIS; BASE SEQUENCE; BCL-2-ASSOCIATED X PROTEIN; BCL-X PROTEIN; DNA; HUMANS; HYDROPHOBICITY; MITOCHONDRIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS C-BCL-2; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE;

INSERTION SEQUENCES;

EID: 10644224222     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M408373200     Document Type: Article

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