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2 results on '"AGPase"'

1. Functional Analysis of a Wheat AGPase Plastidial Small Subunit with a Truncated Transit Peptide.

Author

Yang Yang, Tian Gao, Mengjun Xu, Jie Dong, Hanxiao Li, Pengfei Wang, Gezi Li, Tiancai Guo, Guozhang Kang, and Yonghua Wang

Subjects
*ADP-glucose pyrophosphorylase, *WHEAT, *STARCH synthesis, *GREEN fluorescent protein, *PEPTIDES
Abstract

ADP-glucose pyrophosphorylase (AGPase), the key enzyme in starch synthesis, consists of two small subunits and two large subunits with cytosolic and plastidial isoforms. In our previous study, a cDNA sequence encoding the plastidial small subunit (TaAGPS1b) of AGPase in grains of bread wheat (Triticum aestivum L.) was isolated and the protein subunit encoded by this gene was characterized as a truncated transit peptide (about 50% shorter than those of other plant AGPS1bs). In the present study, TaAGPS1b was fused with green fluorescent protein (GFP) in rice protoplast cells, and confocal fluorescence microscopy observations revealed that like other AGPS1b containing the normal transit peptide, TaAGPS1b-GFP was localized in chloroplasts. TaAGPS1b was further overexpressed in a Chinese bread wheat cultivar, and the transgenic wheat lines exhibited a significant increase in endosperm AGPase activities, starch contents, and grain weights. These suggested that TaAGPS1b subunit was targeted into plastids by its truncated transit peptide and it could play an important role in starch synthesis in bread wheat grains. [ABSTRACT FROM AUTHOR]

Published
2017
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2. Functional Analysis of a Wheat AGPase Plastidial Small Subunit with a Truncated Transit Peptide

Author

Mengjun Xu, Tian Gao, Tiancai Guo, Jie Dong, Han-Xiao Li, Yang Yang, Gezi Li, Pengfei Wang, Guozhang Kang, and Yonghua Wang

Subjects
0106 biological sciences, 0301 basic medicine, AGPase, Starch, Recombinant Fusion Proteins, Protein subunit, Pharmaceutical Science, Glucose-1-Phosphate Adenylyltransferase, Biology, 01 natural sciences, Analytical Chemistry, Green fluorescent protein, Endosperm, lcsh:QD241-441, 03 medical and health sciences, chemistry.chemical_compound, lcsh:Organic chemistry, Transit Peptide, Complementary DNA, Drug Discovery, Botany, Plastids, Physical and Theoretical Chemistry, Plastid, Triticum, Triticum aestivum L, plastidial small subunit, Communication, starch, Organic Chemistry, digestive, oral, and skin physiology, food and beverages, Chloroplast, Protein Subunits, Protein Transport, 030104 developmental biology, chemistry, Biochemistry, Chemistry (miscellaneous), Proteolysis, Molecular Medicine, Peptides, 010606 plant biology & botany
Abstract

ADP-glucose pyrophosphorylase (AGPase), the key enzyme in starch synthesis, consists of two small subunits and two large subunits with cytosolic and plastidial isoforms. In our previous study, a cDNA sequence encoding the plastidial small subunit (TaAGPS1b) of AGPase in grains of bread wheat (Triticum aestivum L.) was isolated and the protein subunit encoded by this gene was characterized as a truncated transit peptide (about 50% shorter than those of other plant AGPS1bs). In the present study, TaAGPS1b was fused with green fluorescent protein (GFP) in rice protoplast cells, and confocal fluorescence microscopy observations revealed that like other AGPS1b containing the normal transit peptide, TaAGPS1b-GFP was localized in chloroplasts. TaAGPS1b was further overexpressed in a Chinese bread wheat cultivar, and the transgenic wheat lines exhibited a significant increase in endosperm AGPase activities, starch contents, and grain weights. These suggested that TaAGPS1b subunit was targeted into plastids by its truncated transit peptide and it could play an important role in starch synthesis in bread wheat grains.

Published
2017

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