TY - JOUR
T1 - Quality control of photosystem II
T2 - Impact of light and heat stresses
AU - Yamamoto, Yasusi
AU - Aminaka, Ryota
AU - Yoshioka, Miho
AU - Khatoon, Mahbuba
AU - Komayama, Keisuke
AU - Takenaka, Daichi
AU - Yamashita, Amu
AU - Nijo, Nobuyoshi
AU - Inagawa, Kayo
AU - Morita, Noriko
AU - Sasaki, Takayuki
AU - Yamamoto, Yoko
N1 - Funding Information:
Acknowledgments This work was supported by a Grant-in-Aid for Scientific Research (20570039) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, the Wesco Science Promotion Foundation, and the Ryobi Foundation to Yasusi Yamamoto.
PY - 2008/10
Y1 - 2008/10
N2 - Photosystem II is vulnerable to various abiotic stresses such as strong visible light and heat. Under both stresses, the damage seems to be triggered by reactive oxygen species, and the most critical damage occurs in the reaction center-binding D1 protein. Recent progress has been made in identifying the protease involved in the degradation of the photo- or heat-damaged D1 protein, the ATP-dependent metalloprotease FtsH. Another important result has been the discovery that the damaged D1 protein aggregates with nearby polypeptides such as the D2 protein and the antenna chlorophyll-binding protein CP43. The degradation and aggregation of the D1 protein occur simultaneously, but the relationship between the two is not known. We suggest that phosphorylation and dephosphorylation of the D1 protein, as well as the binding of the extrinsic PsbO protein to Photosystem II, play regulatory roles in directing the damaged D1 protein to the two alternative pathways.
AB - Photosystem II is vulnerable to various abiotic stresses such as strong visible light and heat. Under both stresses, the damage seems to be triggered by reactive oxygen species, and the most critical damage occurs in the reaction center-binding D1 protein. Recent progress has been made in identifying the protease involved in the degradation of the photo- or heat-damaged D1 protein, the ATP-dependent metalloprotease FtsH. Another important result has been the discovery that the damaged D1 protein aggregates with nearby polypeptides such as the D2 protein and the antenna chlorophyll-binding protein CP43. The degradation and aggregation of the D1 protein occur simultaneously, but the relationship between the two is not known. We suggest that phosphorylation and dephosphorylation of the D1 protein, as well as the binding of the extrinsic PsbO protein to Photosystem II, play regulatory roles in directing the damaged D1 protein to the two alternative pathways.
KW - D1 protein
KW - FtsH proteases
KW - Light stress and heat stress
KW - Photosystem II
KW - PsbO protein
KW - Reactive oxygen species
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U2 - 10.1007/s11120-008-9372-4
DO - 10.1007/s11120-008-9372-4
M3 - Review article
C2 - 18937045
AN - SCOPUS:57849134955
SN - 0166-8595
VL - 98
SP - 589
EP - 608
JO - Photosynthesis research
JF - Photosynthesis research
IS - 1-3
ER -