硅藻光合系统 I 超级复合物中的叶绿素 a/c 结合蛋白分子组装的结构基础。

IF 6.4 1区 生物学 Q1 BIOLOGY
eLife Pub Date : 2024-10-31 DOI:10.7554/eLife.99858
Koji Kato, Yoshiki Nakajima, Jian Xing, Minoru Kumazawa, Haruya Ogawa, Jian-Ren Shen, Kentaro Ifuku, Ryo Nagao
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引用次数: 0

摘要

光合生物的采光复合物(LHC)具有显著的多样性。LHC 与光系统 I(PSI)相关联,形成 PSI-LHCI 超级复合物。在 PSI-LHCI 结构中,LHCI 亚基的数量、蛋白质序列和色素组成都有很大不同。然而,LHCIs 在 PSI 核心内识别其特定结合位点的机制仍不清楚。在这项研究中,我们测定了从硅藻 Thalassiosira pseudonana CCMP1335 中分离出来的包含岩藻黄素叶绿素 a/c 结合蛋白(FCPs)的 PSI 超级复合物(命名为 PSI-FCPI)的冷冻电镜结构。PSI-FCPI 的结构分析表明有五个 FCPI 亚基与 PSI 单体相关联;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 FCPI 和 PSI 亚基之间以及 FCPI 亚基本身之间界面上特定的蛋白质-蛋白质相互作用。对 PSI-FCPI 超级复合物的结构比较分析,结合对来自 T. pseudonana 和硅藻 Chaetoceros gracilis 的 FCPs 的系统发育分析,强调了对单个 FCPI 亚基的选择性结合至关重要的蛋白质基团的进化保守性。这些发现为了解硅藻中 FCPIs 的组装和选择性结合的分子机制提供了重要启示。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structural basis for molecular assembly of fucoxanthin chlorophyll a/c-binding proteins in a diatom photosystem I supercomplex.

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 a/c-binding proteins (FCPs), designated as PSI-FCPI, isolated from the diatom Thalassiosira pseudonana 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 T. pseudonana and the diatom Chaetoceros gracilis, 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.

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来源期刊
eLife
eLife BIOLOGY-
CiteScore
12.90
自引率
3.90%
发文量
3122
审稿时长
17 weeks
期刊介绍: eLife is a distinguished, not-for-profit, peer-reviewed open access scientific journal that specializes in the fields of biomedical and life sciences. eLife is known for its selective publication process, which includes a variety of article types such as: Research Articles: Detailed reports of original research findings. Short Reports: Concise presentations of significant findings that do not warrant a full-length research article. Tools and Resources: Descriptions of new tools, technologies, or resources that facilitate scientific research. Research Advances: Brief reports on significant scientific advancements that have immediate implications for the field. Scientific Correspondence: Short communications that comment on or provide additional information related to published articles. Review Articles: Comprehensive overviews of a specific topic or field within the life sciences.
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