The molecular basis of genetic diversity among cytoplasms of Triticum and Aegilops. VI. Complete nucleotide sequences of the rbcL genes encodign H- and L-type Rubisco large subunits in common wheat and Ae. crassa 4x.

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Abstract
The complete nucleotide sequence of the structural gene for each H- and L-type large subunit (LS) of Rubisco (rbcL), which differ in isoelectric point and are related with the differential in vitro CO2 fixation efficiency of this enzyme, was deterined using cloned chloroplast (ct) DNA fragments of common wheat (Triticum aestivum cv. Chinese Spring; H-type) and Aegilops crassa (4x accession; L-type). Two rbcL genes have almost an identical nucleotide sequence in both the coding and noncoding regions; only five base substituions and two deletions/insertions were detected. The coding region of rbcL gene of T. aestivum consists of 1431 bp that can encode a peptide of 477 amino acids, whereas that Ae. crassa 4x contains 1428 bp, which code for a 476-amino acid peptide. Compared to the L-type LS of Ae. crass, the H-type Ls of T. aestivum is assumed to have two amino acid substitutions (Gln .fwdarw. Lys, Asn .fwdarw. Ser) and one amino acid addition (Lys) to the C terminus. This supposition is consistent with the finding that the isoelectric point of the H-type LS is higher than that of the L-type LS. The replacement of Gln in the L-type LS with Lys in the H-type LS is the most plausible amino acid change that causes a great difference in the specific actiivty between the Rubisco with the H- and L-type LS.