Characterisation of three cDNA clones encoding different mRNAs for the precursor to the small subunit of wheat ribolosebisphosphate carboxylase

We have isolated and sequenced three cDNA clones for the nuclear encoded precursor to the small subunit of the chloroplast enzyme, ribulose- 1,5-bisphosphate carboxylase of wheat. The nucleotide sequences of these clones are different, indicating that they are probably derived from three different mRNAs. This finding is consistent with the proposal that this polypeptide is encoded by a multigene family in wheat, in support of similar data reported by Broglie et al. (Bio/Technology 1:55-61, 1983). We deduce that the mature small subunit polypeptide is comprised of 128 amino acids and that its precursor contains an N-terminal transit peptide sequence. The sequences of both the mature small subunit and its transit peptide differ at several positions from those determined by Broglie et al. (1983) from a different wheat cultivar. Different wheat cultivars might therefore contain different small subunit polypeptides. A comparison of nucleotide and amino acid sequences of the small subunit from wheat, pea, soybean 'and spinach shows that these sequences are not highly conserved, particularly between monocotyledon and dicotyledon species.