Quality control of photosystem II: Impact of light and heat stresses

Yasusi Yamamoto, Ryota Aminaka, Miho Yoshioka, Mahbuba Khatoon, Keisuke Komayama, Daichi Takenaka, Amu Yamashita, Nobuyoshi Nijo, Kayo Inagawa, Noriko Morita, Takayuki Sasaki, Yoko Yamamoto

Research output: Contribution to journalReview articlepeer-review

186 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)589-608
Number of pages20
JournalPhotosynthesis research
Issue number1-3
Publication statusPublished - Oct 2008


  • D1 protein
  • FtsH proteases
  • Light stress and heat stress
  • Photosystem II
  • PsbO protein
  • Reactive oxygen species

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology


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