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  • Title: Expression of barley ADP-glucose pyrophosphorylase in Escherichia coli: processing and regulatory considerations.
    Author: Luo C, Kleczkowski LA.
    Journal: Phytochemistry; 1999 Jan; 50(2):209-14. PubMed ID: 9933946.
    Abstract:
    Full length cDNAs for barley ADP-glucose pyrophosphorylase (AGPase) coding for the large subunits of the endosperm and leaf homologues of the enzyme (AGPase-S1 and -S2, respectively) and for the small subunit protein from endosperm (AGPase-B1), have been expressed in Escherichia coli. The cDNAs for AGPase-S1 and -S2 required different induction conditions for their maximal expression and they encoded immunologically distinct proteins. The AGPase-S1 that was produced by E. coli had the same M(r) (58 kDa) as the corresponding protein in barley crude endosperm extracts, whereas the bacteria-produced AGPase-S2 (55 kDa) was larger than its counterpart from barley leaf preparations (53 kDa). An enzymatically active AGPase expressed in E. coli from a double construct containing cDNAs for AGPase-S1 and -B1 subunits was insensitive to the activation by 3-phosphoglycerate and to inhibition by inorganic phosphate, similarly to the enzyme in barley endosperm. Neither AGPase-S1 nor -B1 were active when expressed alone in the bacteria. The data are discussed with respect to possible mechanisms of intracellular targeting of immature AGPase-S proteins in barley tissues and regarding previous data on effector regulation of the barley enzyme.
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