|Name:||ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6|
|PubMed (1830479):|| Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I,Tanaka K, Ichihara A. Molecular cloning of cDNA for the import precursor of human coupling factor 6of H(+)-ATP synthase in mitochondria.Biochem Biophys Res Commun. 1991 Jul 31;178(2):793-9. PMID: 1830479 [PubMed - indexed for MEDLINE]|
The nucleotide sequence of the import precursor of coupling factor 6 (factor 6) of human H(+)-ATP synthase has been determined from a recombinant cDNA clone isolated by screening a human kidney cDNA library with a cDNA for rat factor 6 as a probe. The sequence was composed of 466 nucleotides including a coding region for the import precursor of factor 6 and noncoding regions on the 5'- and 3'-sides. The import precursor of factor 6 and its mature polypeptide deduced from the open reading frame were found to consist of 108 and 76 amino acid residues with molecular weights of 12,596 and 8,969, respectively. The presequence of 32 amino acids could be the import signal peptide for directing the protein into the mitochondrial matrix.
|PubMed (1825642):|| Javed AA, Ogata K, Sanadi DR. Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encodedprecursor of coupling factor 6.Gene. 1991 Jan 15;97(2):307-10. PMID: 1825642 [PubMed - indexed for MEDLINE]|
Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. A human fetal muscle cDNA clone encoding this protein was isolated by screening a lambda gt10 library with oligodeoxyribonucleotide probes. The 497-bp F6 cDNA included a 96-bp segment that delineated a presequence of 32 amino acids (aa) in the precursor protein, and 140 bp of 3'-untranslated sequence. The remainder of the cDNA sequence coded for a mature human F6 protein of 76 aa. The deduced primary aa sequence showed 81% homology to that of bovine F6, differing in 14 aa. Almost all of these aa substitutions were conservative and comparison of the hydropathy profiles revealed a similar pattern.