Scholarlink

<p>Photosystem II (PSII) is essential for energy conversion during oxygenic photosynthesis in plants and algae. <i>Chlorella ohadii</i>, one of the fastest multiplying green algae, thrives under the harsh desert sun but lacks the standard PSII photoprotective mechanisms involving LhcSR/PsbS proteins or protein phosphorylation. Here, we present the cryo-EM structure of the PSII supercomplex from <i>C. ohadii</i> at 2.9 Å resolution, which is used to determine whether the exceptional resistance to desert conditions has a structural basis in PSII. The structure reveals a distinct PsbO isoform and additional subunits, PsbR and PsbY, which enhance core complex stability through extensive interactions. Furthermore, the trimeric light-harvesting complexes (LHCII) are bound to the PSII core by specific light-harvesting proteins whose down-regulation in response to high-light conditions implies a reduction in the number of bound LHCII trimers. These structural modifications, together with the high accumulation of specific polyamines in the thylakoid membrane, play a key role in maintaining PSII stability and photoprotection, allowing <i>C. ohadii</i> to survive in extreme conditions.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年1月9日

查看全文
  • Rameez Arshad,
  • Ioannis Skalidis,
  • David Kopečný,
  • Sylva Brabencová,
  • Monika Opatíková,
  • Petr Ilík,
  • Pavel Pospíšil,
  • Farzad Hamdi,
  • Sanja Ćavar Zeljković,
  • Martina Kopečná,
  • Pavel Roudnický,
  • Dušan Lazár,
  • Eduard Elias,
  • Roberta Croce,
  • Panagiotis L. Kastritis,
  • Roman Kouřil

摘要

Photosystem II (PSII) is essential for energy conversion during oxygenic photosynthesis in plants and algae. Chlorella ohadii, one of the fastest multiplying green algae, thrives under the harsh desert sun but lacks the standard PSII photoprotective mechanisms involving LhcSR/PsbS proteins or protein phosphorylation. Here, we present the cryo-EM structure of the PSII supercomplex from C. ohadii at 2.9 Å resolution, which is used to determine whether the exceptional resistance to desert conditions has a structural basis in PSII. The structure reveals a distinct PsbO isoform and additional subunits, PsbR and PsbY, which enhance core complex stability through extensive interactions. Furthermore, the trimeric light-harvesting complexes (LHCII) are bound to the PSII core by specific light-harvesting proteins whose down-regulation in response to high-light conditions implies a reduction in the number of bound LHCII trimers. These structural modifications, together with the high accumulation of specific polyamines in the thylakoid membrane, play a key role in maintaining PSII stability and photoprotection, allowing C. ohadii to survive in extreme conditions.