Nucleotide Sequence of cDNA Encoding the Small Subunit of Ribolose-1,5-Bisphosphate Carboxylase from Maize1

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Abstract
We have cloned a full length cDNA for the small subunit of ribulose-l,5-bisphosphate carboxylase from C4 mońocot maize, determined the complete nucleotide sequence of this cDNA and deduced its amino acid sequence. The cDNA insert included 513 bp of the coding region, and 65 and 252 nucleotides of the 5′ and 3′ untranslated regions, respectively. The transit and mature peptides have, respectively, 47 and 123 amino acids. Comparison with the small subunit genes from other plants revealed that the maize small subunit is similar to the wheat one, there being 73 % homology between the transit peptides and 64% between the mature proteins. This indicates that there is no noteworthy difference between the C3 and c4 small subunit structures. Extreme codon bias was observed for this gene, and similar codon preferences are observed for other proteins highly expressed in maize leaf, light harvesting chlorophyll binding protein and phosphoenolpyruvate carboxylase. The results indicate that preferential codon usage for highly expressed genes occurs in maize leaf.