Falson, P.
Leterme, S.
Capiau, C.
Boutry, Marc
[UCL]
The Schizosaccharomyces pombe nuclear gene, atp2, encoding the beta subunit of the mitochondrial ATP synthase, was sequenced and found to contain a 1575-bp open reading frame. Two adjacent transcription-initiation sites were found at positions 34 and 44 nucleotides upstream of the translation-initiation codon. The deduced polypeptide sequence was composed of 525 amino acid residues (molecular mass = 56875 Da). The mature polypeptide starts at residue 45 (molecular mass = 51,685 Da), indicating the presence of a presequence of 44 residues, presumably involved in mitochondrial targeting. The atp2 mutant B59-1 [Boutry, M. & Goffeau, A. (1982) Eur. J. Biochem. 125, 471-477] and its related revertant allele R4-3 [Jault, J. M., Di Pietro, A., Falson, P., Gautheron, D. C., Boutry, M. & Goffeau, A. (1989) Biochem. Biophys. Res. Commun. 158, 392-399] were also cloned and sequenced. A single nonsense mutation, CAG (Gln170)----TAG (stop) in mutant B59-1, became a missense mutation, TAG (stop)----TAC (Tyr) in revertant R4-3. Gln170 is located between the first and second elements belonging to the nucleotide-binding site. Its substitution by a tyrosine residue increases the enzyme affinity towards ADP, the amount of endogenous nucleotides and the apparent negative cooperativity for ATPase activity.
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Bibliographic reference |
Falson, P. ; Leterme, S. ; Capiau, C. ; Boutry, Marc. Beta subunit of mitochondrial F1-ATPase from the fission yeast. Deduced sequence of the wild type protein and identification of a mutation that increases nucleotide binding. In: European Journal of Biochemistry / FEBS, Vol. 200, no. 1, p. 61-7 (1991) |
Permanent URL |
http://hdl.handle.net/2078.1/11310 |