TY - JOUR
T1 - Quality control of Photosystem II
T2 - The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes
AU - Yoshioka-Nishimura, Miho
AU - Yamamoto, Yasusi
N1 - Funding Information:
We thank Drs. Yuichiro Takahashi and Jian-Ren Shen of Okayama University for valuable discussions and Ms. Noriko Morita for preparing figures. Thanks are also due to Dr. Takashi Takaki of JEOL, Tokyo, Japan for his kind assistance in electron microscopy. This work was supported by a Grant-in-Aid for Scientific Research 24570053 from the Ministry of Education, Culture, Sports, Science and Technology of Japan to Y.Y., and grants for the Okayama University Woman–Tenure–Track (WTT) Staff from Okayama University, from the Japan Science Society (The Sasakawa Scientific Research Grant), from the Ryobi Foundation, and from the Nippon Life Insurance Foundation to M.Y.-N.
PY - 2014/8
Y1 - 2014/8
N2 - The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II.
AB - The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II.
KW - FtsH protease
KW - Grana
KW - Light stress
KW - Photosystem II
KW - Thylakoid
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U2 - 10.1016/j.jphotobiol.2014.02.012
DO - 10.1016/j.jphotobiol.2014.02.012
M3 - Review article
C2 - 24725639
AN - SCOPUS:84904258587
SN - 1011-1344
VL - 137
SP - 100
EP - 106
JO - Journal of Photochemistry and Photobiology B: Biology
JF - Journal of Photochemistry and Photobiology B: Biology
ER -