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Subunits of mitochondrial H-ATPases are investigated under a variety of different aspects: (i) mechanisms of energy coupling (1, 2); (ii) evolution of ATPases (3) and (iii) mechanisms of mitochondrial import and assembly of the nuclear coded subunits (4—7). For the latter reason, we have cloned and expressed a full-length cDNA coding for the nuclear coded /8-subunit of the Fj-ATPase from Neurospora crassa. The nucleotide sequence and the deduced amino acid sequence are shown in Figure 1. The protein is synthesized in the cytosol as a precursor of 55,470 Da which is cleaved inside mitochondria to the mature protein. The mature protein shares 70 — 80% of sequence similarity to known mitochondrial /3 subunits, for example yeast (8), bovine (9) or human (10).

nucleic acids research

Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the β-subunit of F<sub>1</sub>-ATPase from<i>Neurospora crassa</i>

Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the β-subunit of F1-ATPase fromNeurospora crassa

Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the β-subunit of F₁-ATPase fromNeurospora crassa