Abstract
λgt10 cDNA clones for the nuclear encoded subunit δ of chloroplast ATP-synthase from Pisum sativum have been isolated. The 5′ end was completed by PCR. The sequenced cDNA codes for the import precursor. N-Terminal sequencing of the mature protein isolated from chloroplasts revealed that the processing sites of the transit peptide from Pisum sativum and Spinacea oleracea are similar. The overall homology of the deduced amino acid sequences of the mature δ proteins from higher plants is about 40%. The conservation among hydrophilic residues is higher than for hydrophobic ones, indicating that the surface of δ is important for its function within the ATP-synthase.
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