N-terminal sequence of the rat liver beta-subunit in the mitochondrial ATPase-ATPsynthase.
The N-terminal amino acid residues of the beta-subunit in the rat liver mitochondrial ATPase - ATPsynthase have been identified by direct microsequencing after electrophoresis of either purified F1 or F0F1. The mature rat liver beta-subunit begins by two alanine residues that precede the glutamine recently proposed as the first amino acid of the sequence (Boulet, D., Poirier, J. and Côté, C., 1989, Biochem. Biophys. Res. Commun. 159, 1184-1190). This result indicates that the proteolytic cleavage of the beta-subunit precursor may occur at the level of this first alanine. This may be important in the understanding of proteolytic processing events which lead to the assembly of the ATPase-ATPsynthase subunits during mitochondrial biogenesis.
Cretin
F
F
Laboratoire de Biologie et Technologie des membranes du CNRS, Université Claude Bernard de Lyon, Villeurbanne, France.
Baggetto
L G
LG
Denoroy
L
L
Godinot
C
C
D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008930:Mitochondria, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D006180:Proton-Translocating ATPases / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases