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结构基础的分子组装的岩藻黄素叶绿素 / - 结合蛋白在一个硅藻光系统 I 超复合体。

Structural basis for molecular assembly of fucoxanthin chlorophyll /-binding proteins in a diatom photosystem I supercomplex.

机构信息

Research Institute for Interdisciplinary Science and Graduate School of Environmental, Life, Natural Science and Technology, Okayama University, Okayama, Japan.

Graduate School of Agriculture, Kyoto University, Kyoto, Japan.

出版信息

Elife. 2024 Oct 31;13:RP99858. doi: 10.7554/eLife.99858.

DOI:10.7554/eLife.99858
PMID:39480899
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11527431/
Abstract

Photosynthetic organisms exhibit remarkable diversity in their light-harvesting complexes (LHCs). LHCs are associated with photosystem I (PSI), forming a PSI-LHCI supercomplex. The number of LHCI subunits, along with their protein sequences and pigment compositions, has been found to differ greatly among the PSI-LHCI structures. However, the mechanisms by which LHCIs recognize their specific binding sites within the PSI core remain unclear. In this study, we determined the cryo-electron microscopy structure of a PSI supercomplex incorporating fucoxanthin chlorophyll /-binding proteins (FCPs), designated as PSI-FCPI, isolated from the diatom CCMP1335. Structural analysis of PSI-FCPI revealed five FCPI subunits associated with a PSI monomer; these subunits were identified as RedCAP, Lhcr3, Lhcq10, Lhcf10, and Lhcq8. Through structural and sequence analyses, we identified specific protein-protein interactions at the interfaces between FCPI and PSI subunits, as well as among FCPI subunits themselves. Comparative structural analyses of PSI-FCPI supercomplexes, combined with phylogenetic analysis of FCPs from and the diatom , underscore the evolutionary conservation of protein motifs crucial for the selective binding of individual FCPI subunits. These findings provide significant insights into the molecular mechanisms underlying the assembly and selective binding of FCPIs in diatoms.

摘要

光合生物在其光捕获复合物（LHCs）中表现出显著的多样性。LHCs 与光系统 I（PSI）相关联，形成 PSI-LHCI 超复合物。已经发现，PSI-LHCI 结构中的 LHCI 亚基的数量、其蛋白质序列和色素组成存在很大差异。然而，LHCIs 如何识别其在 PSI 核心内的特定结合位点的机制尚不清楚。在这项研究中，我们确定了来自硅藻 CCMP1335 的 PSI 超复合物结合岩藻黄素叶绿素/-结合蛋白（FCPs）的冷冻电子显微镜结构，命名为 PSI-FCPI。PSI-FCPI 的结构分析揭示了与 PSI 单体结合的五个 FCP 亚基；这些亚基被鉴定为 RedCAP、Lhcr3、Lhcq10、Lhcf10 和 Lhcq8。通过结构和序列分析，我们确定了 FCP 和 PSI 亚基之间以及 FCP 亚基自身之间的特定蛋白-蛋白相互作用。PSI-FCPI 超复合物的比较结构分析，结合来自 和硅藻的 FCPs 的系统发育分析，强调了对于个体 FCP 亚基选择性结合至关重要的蛋白质模体的进化保守性。这些发现为硅藻中 FCPIs 的组装和选择性结合的分子机制提供了重要的见解。

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