Kumika Kondo
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Kumika Kondo has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
Arisa Terada
Graduate School of Science and Engineering, Saitama University , 255 Shimo-Okubo, Saitama 338-8570 , Japan
1 shared publication- Kakeru Suzuki
Graduate School of Science and Engineering, Saitama University , 255 Shimo-Okubo, Saitama 338-8570 , Japan
1 shared publication - Riku Nakamura
Graduate School of Science and Engineering, Saitama University , Saitama, 338-8570
1 shared publication - Shogo Tachibana
Graduate School of Science and Engineering, Saitama University , 255 Shimo-Okubo, Saitama 338-8570 , Japan
1 shared publication - Yuji Takahashi
Graduate School of Science and Engineering, Saitama University , 255 Shimo-Okubo, Saitama 338-8570 , Japan
1 shared publication - Yukako Hihara
Graduate School of Science and Engineering, Saitama University, Saitama, Japan
1 shared publication
Latest Publications
- 4 June 2024
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 196 (1) , 621-633
Partner-switching components PmgA and Ssr1600 regulate high-light acclimation in Synechocystis sp. PCC 6803
Photomixotrophic growth A (PmgA) is a pleiotropic regulator essential for growth under photomixotrophic and prolonged high-light (HL) conditions in the cyanobacterium Synechocystis sp. PCC 6803. The overall similarity with the anti-sigma factor of the bacterial partner-switching system indicates that PmgA exerts a regulatory function via phosphorylation of its target proteins. In this study, we performed an in vitro phosphorylation assay and protein-protein interaction analysis and found that PmgA interacts with four anti-sigma antagonist homologs, Ssr1600, Slr1856, Slr1859, and Slr1912, but specifically phosphorylates Ssr1600. Phenotypic analyses using the set of gene disruption and overexpression strains of pmgA and ssr1600 revealed that phosphorylation by PmgA is essential for the accumulation of Ssr1600 protein in vivo. The ssr1600-disrupted mutant showed similar phenotypes as those previously reported for the pmgA-disrupted mutant, namely, no obvious phenotype just after the shift to HL, but higher chlorophyll content, 5-aminolevulinic acid synthesis activity, and psaAB transcript levels than those in the wild-type after 6 hours. These findings indicate that the phosphorylated form of Ssr1600 works as the output of the partner-switching system to coordinately repress chlorophyll biosynthesis and accumulation of photosystem I during HL acclimation.
- 4 June 2024
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 196 (1) , 621-633
Partner-switching components PmgA and Ssr1600 regulate high-light acclimation in Synechocystis sp. PCC 6803
Photomixotrophic growth A (PmgA) is a pleiotropic regulator essential for growth under photomixotrophic and prolonged high-light (HL) conditions in the cyanobacterium Synechocystis sp. PCC 6803. The overall similarity with the anti-sigma factor of the bacterial partner-switching system indicates that PmgA exerts a regulatory function via phosphorylation of its target proteins. In this study, we performed an in vitro phosphorylation assay and protein-protein interaction analysis and found that PmgA interacts with four anti-sigma antagonist homologs, Ssr1600, Slr1856, Slr1859, and Slr1912, but specifically phosphorylates Ssr1600. Phenotypic analyses using the set of gene disruption and overexpression strains of pmgA and ssr1600 revealed that phosphorylation by PmgA is essential for the accumulation of Ssr1600 protein in vivo. The ssr1600-disrupted mutant showed similar phenotypes as those previously reported for the pmgA-disrupted mutant, namely, no obvious phenotype just after the shift to HL, but higher chlorophyll content, 5-aminolevulinic acid synthesis activity, and psaAB transcript levels than those in the wild-type after 6 hours. These findings indicate that the phosphorylated form of Ssr1600 works as the output of the partner-switching system to coordinately repress chlorophyll biosynthesis and accumulation of photosystem I during HL acclimation.