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ADP-glucose pyrophosphorylase (AGP) consists of two large (AGP-L) and two small (AGP-S) subunits; it regulates the limiting step in the biosynthesis of starch. Here, we isolated the full-length cDNA sequence of the AGP-S gene (designed as  Agp1 ) from wheat and whole genomic sequences from relatives of wheat. The coding region of  Agp1  ranged from 5948 bp to 7666 bp and contained 9 exons and 8 introns. The full-length cDNA sequence of  Agp1  encoded a polypeptide containing 473 amino acids without transit peptides. The sequence alignment and phylogenetic tree analyses indicated that the  Agp1  cDNA sequence was highly conserved (99.7%) across the diploid Triticeae species examined in this study. Variations in introns caused the  Agp1  genomic sequences from wheat relatives to be less similar (79.5%), and  Agp1  sequences from the B genome donor species were divergent. In developing grains, rapid increase in  Agp1  expression at prophase was closely followed by the accumulation of starch, and a significant ( P  &lt; 0.001) correlation was observed between them. The heterogeneous mixtures of small and large subunits from different wheat species restarted glycogen synthesis in the  Escherichia coli  AC70R1-504 cells, which are deficient in endogenous AGP activity ( glg  C −/− ). Our data provide useful information to evaluate and utilize  Agp1  sequences in Triticeae species.

Cloning and characterization of Agp1 , the gene encoding the small subunit of ADP-glucose pyrophosphorylase from wheat and its relatives