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

Komatsu, Setsuko; Masuda, Takanori; Hirano, Hisashi

doi:10.1016/0014-5793(96)00275-x

Cited by 27 publications

(9 citation statements)

References 21 publications

(26 reference statements)

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“…However, some studies have reported that RCA quickly responds to stress conditions and treatment with plant hormone, which is quite different from the functions of Rubisco activation of RCA accepted by most researchers. Komatsu et al [ 40 ] reported that a gibberellin-binding protein in rice is homologous to RCA, and Sharma and Komatsu [ 41 ] suggested that RCA is associated with Ca 2+ -dependent protein kinases in gibberellin signaling. Dejimenez et al [ 42 ] first reported that 45 kD RCA L is induced at high temperature (45°C) and disappears at normal temperature.…”

Section: Discussionmentioning

confidence: 99%

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

et al. 2015

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Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is a nuclear gene that encodes a chloroplast protein that plays an important role in photosynthesis. Some reports have indicated that it may play a role in acclimation to different abiotic stresses. In this paper, we analyzed the stress-responsive elements in the 2.0 kb 5’-upstream regions of the RCA gene promoter and the primary, secondary and tertiary structure of the protein. We identified some cis-elements of multiple stress-related components in the RCA promoter. Amino acid and evolution analyses showed that the RCA protein had conserved regions between different species; however, the size and type varied. The secondary structures, binding sites and tertiary structures of the RCA proteins were also different. This might reflect the differences in the transcription and translation levels of the two RCA isoforms during adaptation to different abiotic stresses. Although both the transcription and translation levels of RCA isoforms in the rice leaves increased under various stresses, the large isoform was increased more significantly in the chloroplast stroma and thylakoid. It can be concluded that RCA, especially RCAL, is also a multiple responder to abiotic stresses in rice, which provides new insights into RCA functions.

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Section: Discussionmentioning

confidence: 99%

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

et al. 2015

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“…25) RuBisCO activase has recently been shown to function as the GA-binding protein in rice, 26) inducing two independent cytosolic Ca 2ϩ -dependent protein kinase signaling components downstream to the RuBisCO, and suggesting their role in GA signaling. 27) LS208 matched the elongation factor from Taxeobacter ocellatus; this elongation factor promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Proteins Responsive to Gibberellin in the Leaf-Sheath of Rice (Oryza sativa L.) Seedling Using Proteome Analysis.

Shen

Sharma

Komatsu

2003

Biological & Pharmaceutical Bulletin

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“…Although several GA‐binding proteins have been identified from different plants including maize (Keith & Rappaport 1987), bean (Nakajima et al . 1997), rice (Komatsu, Matsuda & Hirano 1996b), oat, pea and Arabidopsis (Lovegrove et al . 1998), their functions remain to be identified.…”

Section: Introductionmentioning

confidence: 99%

A gibberellin‐regulated protein phosphorylated by a putative Ca²⁺‐dependent protein kinase is G‐protein mediated in rice root

Khan

Yang

Iwasaki

et al. 2005

Plant Cell & Environment

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The GA-signal transduction pathways downstream to the Ga a a a protein in rice seedling root were investigated using ingel kinase assay and in vitro protein phosphorylation techniques with a Ga a a a protein defective mutant, d1. A 50-kDa protein kinase was detected downstream to Ga a a a protein in the membrane fraction of rice seedling roots using an ingel kinase assay with histone III-S as a substrate. The activity of a 50-kDa protein kinase increased in the wild-type rice by gibberellin (GA 3 ) treatment, but did not change in the d1 mutant. This protein kinase activity was inhibited by the Ca 2 + chelator ethyleneglycol-bis-(beta-aminoethylether)-N , N , N 1 , N 1 -tetraacetic acid (EGTA), protein kinase inhibitors, staurosporine and H7, and calmodulin antagonist, trifluoperazine, suggesting that the 50-kDa protein kinase is a putative plant Ca 2 + -dependent protein kinase (CDPK). The activity of the 50-kDa putative CDPK reached its highest level at 3 h after GA 3 treatment and then gradually declined with time. In order to identify the endogenous substrate for 50-kDa putative CDPK, two-dimensional polyacrylamide gel electrophoresis followed by in vitro protein phosphorylation was carried out. The phosphorylation activity of an endogenous protein PP30, identified as an unknown protein having molecular weight 30 kDa and isoelectric point 5.8 was increased in the wild-type rice by GA 3 treatment, compared with the d1 mutant. The addition of GA 3 treated membrane fraction, which predominantly represent a 50-kDa putative CDPK further increased the phosphorylation of PP30. Almost similar to GA 3 treatment, phosphorylation activity of PP30 was also increased by the treatment with cholera toxin in the wild-type rice but not in d1 mutant. These results suggest that the 50-kDa putative CDPK and an unknown protein, PP30 promoted by GA 3 treatment are G-protein mediated in rice seedling roots.

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

Cited by 27 publications

References 21 publications

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

Characterization of Proteins Responsive to Gibberellin in the Leaf-Sheath of Rice (Oryza sativa L.) Seedling Using Proteome Analysis.

A gibberellin‐regulated protein phosphorylated by a putative Ca²⁺‐dependent protein kinase is G‐protein mediated in rice root

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

Cited by 27 publications

References 21 publications

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

Characterization of Proteins Responsive to Gibberellin in the Leaf-Sheath of Rice (Oryza sativa L.) Seedling Using Proteome Analysis.

A gibberellin‐regulated protein phosphorylated by a putative Ca2+‐dependent protein kinase is G‐protein mediated in rice root

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A gibberellin‐regulated protein phosphorylated by a putative Ca²⁺‐dependent protein kinase is G‐protein mediated in rice root