{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang Y"],"funding":["National Transgenic Major Project","National Natural Science Foundation of China","Program for Science &amp;amp; Technology Innovation Talents in Universities of Henan Province","Independent Item of the National Key Laboratory of Wheat and Maize Crop Science"],"pagination":["E386"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6155376"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(3)"],"pubmed_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 (<i>Triticum aestivum</i> 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 Chines"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Functional Analysis of a Wheat AGPase Plastidial Small Subunit with a Truncated Transit Peptide."],"pmcid":["PMC6155376"],"funding_grant_id":["SKL2014ZH-03","2016ZX08002-003-04","15HASIT029","31571575"],"pubmed_authors":["Li G","Li H","Yang Y","Xu M","Wang P","Kang G","Dong J","Guo T","Wang Y","Gao T"],"additional_accession":[]},"is_claimable":false,"name":"Functional Analysis of a Wheat AGPase Plastidial Small Subunit with a Truncated Transit Peptide.","description":"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 (<i>Triticum aestivum</i> 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 Chines","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Mar","modification":"2026-05-02T10:22:25.096Z","creation":"2026-04-07T17:53:01.98Z"},"accession":"S-EPMC6155376","cross_references":{"pubmed":["28257051"],"doi":["10.3390/molecules22030386"]}}