Rice gibberellin-binding phosphoprotein structurally related to ribulose-1,5-bisphosphate carboxylase/oxygenase activase.
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-biphosphate 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 Ca2+, Mg2+ and ATP in the leaf protein extracts of rice grown in the presence of exogenous GA.
Komatsu
S
S
Department of Molecular Biology, National Institute of Agrobiological Resources, Ibaraki, Japan.
Masuda
T
T
Hirano
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002696:Chlamydomonas / Q000201:enzymology; D015180:Electrophoresis, Gel, Two-Dimensional; D001467:Hordeum / Q000201:enzymology; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D012275:Oryza / Q000378:metabolism*; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D018724:Spinacia oleracea / Q000201:enzymology
D002352:Carrier Proteins; D010750:Phosphoproteins; D010940:Plant Proteins; C099131:gibberellin-binding phosphoprotein, plant; D012273:Ribulose-Bisphosphate Carboxylase