Abstract：
:The structure of ATP synthase subunit 4 was determined by using the oligonucleotide probe procedure. This subunit is the fourth polypeptide of the complex when classifying subunits in order of decreasing molecular mass. Its relative molecular mass is 25 kDa. The ATP4 gene was isolated and sequenced. The nucleotide sequence predicts that subunit 4 is probably derived from a precursor protein 244 amino acids long. Mature subunit 4 contains 209 amino acid residues and the predicted molecular mass is 23250 kDa. Subunit 4 shows homology with the b-subunit of Escherichia coli ATP synthase and the b-subunit of beef heart mitochondrial ATP synthase. By using homologous transformation, a mutant lacking wild subunit 4 was constructed. This mutant is devoid of oxidative phosphorylation and F1 is loosely bound to the membrane. Our data are in favor of a structural relationship between subunit 4 and the mitochondrially-translated subunit 6 during biogenesis of F0.
journal_name
Biochimiejournal_title
Biochimieauthors
Velours J,Arselin G,Paul MF,Galante M,Durrens P,Aigle M,Guerin Bdoi
10.1016/0300-9084(89)90073-4subject
Has Abstractpub_date
1989-08-01 00:00:00pages
903-15issue
8eissn
0300-9084issn
1638-6183pii
0300-9084(89)90073-4journal_volume
71pub_type
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