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

Title
Loss-of-function of OsSTN8 suppresses the photosystem II core protein phosphorylation and interferes with the photosystem II repair mechanism in rice (Oryza sativa)
Author(s)
Nath, KrishnaPoudyal, Roshan SharmaEom, Joon-SeobPark, Yu ShinZulfugarov, Ismayil S.Mishra, Sujata R.Tovuu, AltanzayaRyoo, NayeoonYoon, Ho-SungNam, Hong GilAn, GynheungJeon, Jong-SeongLee, Choon-Hwan
Issued Date
2013-11
Citation
Plant Journal, v.76, no.4, pp.675 - 686
Type
Article
Author Keywords
STN8 kinasehigh light illuminationphotosystemII core protein phosphorylationD1 protein degradationphotosystemII repairrice
Keywords
DNA INSERTIONAL MUTAGENESISPHOTOSYNTHETIC MEMBRANESARABIDOPSIS-THALIANASTATE TRANSITIONSQUANTUM YIELDD1 PROTEINLIGHTPHOTOINHIBITIONDEGRADATIONINVOLVEMENT
ISSN
0960-7412
Abstract
STN8 kinase is involved in photosystem II (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. © 2013 The Authors The Plant Journal © 2013 John Wiley & Sons Ltd.
URI
http://hdl.handle.net/20.500.11750/1692
DOI
10.1111/tpj.12331
Publisher
Wiley Blackwell
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Department of New Biology CBRG(Complex Biology Research Group) 1. Journal Articles

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