Abstract
A full-length cDNA clone from hexaploid bread wheat, encoding the small subunit of ADP-glucose pyrophosphorylase, has been isolated from an endosperm cDNA library. The cDNA insert has an open reading frame which encodes a protein of 473 amino acids (52.1 kDa). The presence of a chloroplast/amyloplast transit peptide of 22 amino acids is proposed. The deduced amino acid sequence exhibits a high degree of homology with the small subunit ADP-glucose pyrophosphorylase proteins from rice (with 90% of identical amino acids) and potato (with 86% of identical amino acids) and contains conserved sequence elements which are thought to represent the substrate binding and allosteric activator sites. The genes are organised as single-copy loci on chromosomes 7A, 7B and 7D in the wheat genome and are highly expressed during grain development. Homologous transcripts are expressed in leaves and roots.
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Ainsworth, C., Tarvis, M. & Clark, J. Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat. Plant Mol Biol 23, 23–33 (1993). https://doi.org/10.1007/BF00021416
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DOI: https://doi.org/10.1007/BF00021416