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Background  ADP-glucose pyrophosphorylase (AGPase), the key enzyme in plant starch biosynthesis, is a heterotetramer composed of two identical large subunits and two identical small subunits. AGPase has plastidial and cytosolic isoforms in higher plants, whereas it is mainly detected in the cytosol of grain endosperms in cereal crops. Our previous results have shown that the expression of the  TaAGPL1  gene, encoding the cytosolic large subunit of wheat AGPase, temporally coincides with the rate of starch accumulation and that its overexpression dramatically increases wheat AGPase activity and the rate of starch accumulation, suggesting an important role.    Methods  In this study, we performed yeast one-hybrid screening using the promoter of the  TaAGPL1  gene as bait and a wheat grain cDNA library as prey to screen out the upstream regulators of  TaAGPL1  gene. And the barley stripe mosaic virus-induced gene-silencing (BSMV-VIGS) method was used to verify the functional characterization of the identified regulators in starch biosynthesis.    Results  Disulfide isomerase 1-2 protein (TaPDIL1-2) was screened out, and its binding to the  TaAGPL1 - 1D  promoter was further verified using another yeast one-hybrid screen. Transiently silenced wheat plants of the  TaPDIL1 - 2  gene were obtained by using BSMV-VIGS method under field conditions. In grains of BSMV-VIGS-TaPDIL1-2-silenced wheat plants, the  TaAGPL1  gene transcription levels, grain starch contents, and 1000-kernel weight also significantly increased.    Conclusions  As important chaperones involved in oxidative protein folding, PDIL proteins have been reported to form hetero-dimers with some transcription factors, and thus, our results suggested that TaPDIL1-2 protein could indirectly and negatively regulate the expression of the  TaAGPL1  gene and function in starch biosynthesis.

PDIL1-2 can indirectly and negatively regulate expression of the AGPL1 gene in bread wheat