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GrainGenes Reference Report: PYC-50-209

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Reference	PYC-50-209
Title	Expression of barley ADP-glucose pyrophosphorylase in Escherichia coli: processing and regulatory considerations
Journal	Phytochemistry
Year	1999
Volume	50
Pages	209-214
Author	Luo C Kleczkowski LA
Abstract	Summary: 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 Mr (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 -Bl 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
Keyword	[ Hide all but 1 of 38 ] 3 phosphoglyceric acid activation adp-glucose pyrophosphorylase amino acid sequences barley barley leaves cdna complementary dna distinct endosperm enzyme enzyme activity escherichia coli escherichia-coli expression gene expression gene transfer hordeum vulgare immunochemistry induction inhibition isozymes its kinases leaf leaves length mechanism mechanisms molecular weight nucleotide sequences phosphate phosphates protein protein synthesis proteins regulation tissue

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