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Rice gibberellin‐binding phosphoprotein structurally related to ribulose‐1,5‐bisphosphate carboxylase/oxygenase activase
Author(s) -
Komatsu Setsuko,
Masuda Taizo,
Hirano Hisashi
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00275-x
Subject(s) - ribulose 1,5 bisphosphate , oxygenase , biochemistry , binding protein , phosphoprotein , pyruvate carboxylase , oryza sativa , rubisco , gibberellin , isoelectric point , chemistry , binding site , peptide sequence , biology , enzyme , botany , gene
A gibberellin A (GA)‐binding protein was identified from rice ( Oryza sativa L.) leaves by a ligand‐binding assay. The dissociation constant of GA‐binding protein and GA complex was about 100 nM. This protein has a relative molecular mass of 47 000 and an isoelectric point of 5.1. The partial amino acid sequence of the protein was determined for 54 residues from both the N‐terminal and internal regions. A sequence homology search indicated that the amino acid sequence of GA‐binding protein was homologous to that of the ribulose‐1,5‐bisphosphate carboxylase/oxygenase activase from barley, Arabidopsis , spinach and Chlamydomonas . The GA‐binding protein was immunologically detected in two polypeptides in the protein extract from leaves. The GA‐binding protein identified was phosphorylated with Ca 2+ , Mg 2+ and ATP in the leaf protein extracts of rice grown in the presence of exogenous GA.