Protein phosphorylation in amyloplasts regulates starch branching enzyme activity and protein-protein interactions.

Journal article

Protein phosphorylation in amyloplasts and chloroplasts of Triticum aestivum (wheat) was investigated after the incubation of intact plastids with gamma-(32)P-ATP. Among the soluble phosphoproteins detected in plastids, three forms of starch branching enzyme (SBE) were phosphorylated in amyloplasts (SBEI, SBEIIa, and SBEIIb), and both forms of SBE in chloroplasts (SBEI and SBEIIa) were shown to be phosphorylated after sequencing of the immunoprecipitated (32)P-labeled phosphoproteins using qu...

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Authors: Tetlow, I; Wait, R; Lu, Z; Akkasaeng, R; Bowsher, C

• Publication status: Published
• Journal: Plant cell
• Volume: 16
• Issue: 3
• Pages: 694-708
• Publication date: 2004-03-01
• DOI: 10.1105/tpc.017400
• EISSN: 1532-298X
• ISSN: 1040-4651
• Language: English
• Keywords: Triticum; Plant Proteins; Molecular Weight; Adenosine Diphosphate Glucose; Models, Biological; Phosphorylation; 1,4-alpha-Glucan Branching Enzyme; Plastids; Chloroplasts; Amino Acid Sequence; Molecular Sequence Data