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...

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Bibliographic Details
Published in:FEBS letters 1996-04, Vol.384 (2), p.167-171
Main Authors: Komatsu, Setsuko, Masuda, Taizo, Hirano, Hisashi
Format: Article
Language:English
Subjects:
2D-PAGE, two-dimensional polyacrylamide gel electrophoresis
Amino Acid Sequence
Animals
Carrier Proteins - chemistry
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Chlamydomonas - enzymology
Electrophoresis, Gel, Two-Dimensional
GA, gibberellin
Gibberellin-binding protein
Hordeum - enzymology
Isoelectric Point
Molecular Sequence Data
Oryza - metabolism
Oryza sativa
Phosphoproteins - chemistry
Phosphoproteins - isolation & purification
Phosphoproteins - metabolism
Plant Proteins - metabolism
Protein phosphorylation
PVDF, polyvinylidene difluoride
Ribulose-1,5-bisphosphate carboxylase/oxygenase activase
Ribulose-Bisphosphate Carboxylase - chemistry
Rice leaf
RuBisCO, ribulose-1,5-bisphosphate carboxylase/oxygenase
Sequence Alignment
Sequence Homology, Amino Acid
Spinacia oleracea - enzymology
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)00275-X