4.8 Article

Loss-of-function of OsSTN8 suppresses the photosystem II core protein phosphorylation and interferes with the photosystem II repair mechanism in rice (Oryza sativa)

Journal

PLANT JOURNAL
Volume 76, Issue 4, Pages 675-686

Publisher

WILEY
DOI: 10.1111/tpj.12331

Keywords

STN8 kinase; high light illumination; photosystemII core protein phosphorylation; D1 protein degradation; photosystemII repair; rice

Categories

Funding

  1. National Research Foundation of Korea
  2. Korean Government Ministry of Education Science and Technology [2010-0011395, 2011-0017947, 2012-0004968]
  3. Rural Development Administration of the Korean Ministry of Food, Agriculture, Forestry and Fisheries [PJ00948406]
  4. National Research Foundation of Korea [2010-0020417]
  5. National Research Foundation of Korea [2010-0011395, 2010-0020417] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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STN8 kinase is involved in photosystemII (PSII) core protein phosphorylation (PCPP). To examine the role of PCPP in PSII repair during high light (HL) illumination, we characterized a T-DNA insertional knockout mutant of the rice (Oryza sativa) STN8 gene. In this osstn8 mutant, PCPP was significantly suppressed, and the grana were thin and elongated. Upon HL illumination, PSII was strongly inactivated in the mutants, but the D1 protein was degraded more slowly than in wild-type, and mobilization of the PSII supercomplexes from the grana to the stromal lamellae for repair was also suppressed. In addition, higher accumulation of reactive oxygen species and preferential oxidation of PSII reaction center core proteins in thylakoid membranes were observed in the mutants during HL illumination. Taken together, our current data show that the absence of STN8 is sufficient to abolish PCPP in osstn8 mutants and to produce all of the phenotypes observed in the double mutant of Arabidopsis, indicating the essential role of STN8-mediated PCPP in PSII repair.

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