Rice gibberellin‐binding phosphoprotein structurally related to ribulose‐1,5‐bisphosphate carboxylase/oxygenase activase

FEBS Letters

Masuda, Taizo¹  Komatsu, Setsuko¹  Hirano, Hisashi¹ 

[1]Department of Molecular Biology, National Institute of Agrobiological Resources, 2-1–2 Kannondai, Tsukuba, Ibaraki 305, Japan

关键词: Gibberellin-binding protein;    Protein phosphorylation;    Rice leaf;    Ribulose-1;    5-bisphosphate carboxylase/oxygenase activase;    GA;    gibberellin;    PVDF;    polyvinylidene difluoride;    RuBisCO;    ribulose-1;    5-bisphosphate carboxylase/oxygenase;    2D-PAGE;    two-dimensional polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(96)00275-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺, Mg²⁺ and ATP in the leaf protein extracts of rice grown in the presence of exogenous GA.

【 授权许可】

Unknown