TY - JOUR
T1 - Quality control of Photosystem II
T2 - Cleavage and aggregation of heat-damaged D1 protein in spinach thylakoids
AU - Komayama, Keisuke
AU - Khatoon, Mahbuba
AU - Takenaka, Daichi
AU - Horie, Junko
AU - Yamashita, Amu
AU - Yoshioka, Miho
AU - Nakayama, Yohsuke
AU - Yoshida, Mari
AU - Ohira, Satoshi
AU - Morita, Noriko
AU - Velitchkova, Maya
AU - Enami, Isao
AU - Yamamoto, Yasusi
N1 - Funding Information:
This work was supported in part by grants from the Ministry of Education, Culture, Science, Sports and Technology, Japan, the Wesco Science Promotion Foundation, and by an Excellent Research Project Grant of Okayama University. The authors thank Drs. Y. Takahashi and J.-R. Shen of Okayama University for valuable discussion. Thanks are also due to Dr. C. Spetea who gave us a valuable comment on the release of PsbO, P and Q upon heat treatment in the poster session of the International Meeting “Photosynthesis in the post-genomic era: structure and function of photosystems” where part of the results was presented, and to Prof. D. W. Krogmann of Purdue University for critically reading the manuscript.
Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/6
Y1 - 2007/6
N2 - Moderate heat stress (40 °C, 30 min) on spinach thylakoids induced cleavage of the D1 protein, producing an N-terminal 23-kDa fragment, a C-terminal 9-kDa fragment, and aggregation of the D1 protein. A homologue of Arabidopsis FtsH2 protease, which is responsible for degradation of the damaged D1 protein, was abundant in the stroma thylakoids. Two processes occurred in the thylakoids in response to heat stress: dephosphorylation of the D1 protein in the stroma thylakoids, and aggregation of the phosphorylated D1 protein in the grana. Heat stress also induced the release of the extrinsic PsbO, P and Q proteins from Photosystem II, which affected D1 degradation and aggregation significantly. The cleavage and aggregation of the D1 protein appear to be two alternative processes influenced by protein phosphorylation/dephosphorylation, distribution of FtsH, and intactness of the thylakoids.
AB - Moderate heat stress (40 °C, 30 min) on spinach thylakoids induced cleavage of the D1 protein, producing an N-terminal 23-kDa fragment, a C-terminal 9-kDa fragment, and aggregation of the D1 protein. A homologue of Arabidopsis FtsH2 protease, which is responsible for degradation of the damaged D1 protein, was abundant in the stroma thylakoids. Two processes occurred in the thylakoids in response to heat stress: dephosphorylation of the D1 protein in the stroma thylakoids, and aggregation of the phosphorylated D1 protein in the grana. Heat stress also induced the release of the extrinsic PsbO, P and Q proteins from Photosystem II, which affected D1 degradation and aggregation significantly. The cleavage and aggregation of the D1 protein appear to be two alternative processes influenced by protein phosphorylation/dephosphorylation, distribution of FtsH, and intactness of the thylakoids.
KW - D1 protein
KW - FtsH proteases
KW - Phosphatases
KW - Photosystem II
KW - Protein aggregation
KW - Spinach
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U2 - 10.1016/j.bbabio.2007.05.001
DO - 10.1016/j.bbabio.2007.05.001
M3 - Article
C2 - 17543883
AN - SCOPUS:34249811201
SN - 0005-2728
VL - 1767
SP - 838
EP - 846
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 6
ER -