Cryo-electron tomography reveals the packaging pattern of RuBisCOs in Synechococcus β-carboxysome

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2024-05-31 DOI:10.1016/j.str.2024.05.007

Wen-Wen Kong, Yun Zhu, Heng-Rui Zhao, Kang Du, Rui-Qian Zhou, Bo Li, Feng Yang, Pu Hou, Xia-He Huang, Yuxing Chen, Ying-Chun Wang, Fei Sun, Yong-Liang Jiang, Cong-Zhao Zhou

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Abstract

Carboxysomes are large self-assembled microcompartments that serve as the central machinery of a CO₂-concentrating mechanism (CCM). Biogenesis of carboxysome requires the fine organization of thousands of individual proteins; however, the packaging pattern of internal RuBisCOs remains largely unknown. Here we purified the intact β-carboxysomes from Synechococcus elongatus PCC 7942 and identified the protein components by mass spectrometry. Cryo-electron tomography combined with subtomogram averaging revealed the general organization pattern of internal RuBisCOs, in which the adjacent RuBisCOs are mainly arranged in three distinct manners: head-to-head, head-to-side, and side-by-side. The RuBisCOs in the outermost layer are regularly aligned along the shell, the majority of which directly interact with the shell. Moreover, statistical analysis enabled us to propose an ideal packaging model of RuBisCOs in the β-carboxysome. These results provide new insights into the biogenesis of β-carboxysomes and also advance our understanding of the efficient carbon fixation functionality of carboxysomes.

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低温电子断层扫描揭示 Synechococcus β-羧酶体中 RuBisCOs 的包装模式

羧酶体是一种大型自组装微腔室，是二氧化碳浓缩机制（CCM）的核心机构。羧酶体的生物生成需要数千种单个蛋白质的精细组织；然而，内部 RuBisCOs 的包装模式在很大程度上仍然未知。在此，我们纯化了拉长鞘球藻（Synechococcus elongatus PCC 7942）完整的β-羧酶体，并通过质谱鉴定了其中的蛋白质成分。低温电子断层扫描结合子图平均法揭示了内部 RuBisCOs 的一般组织模式，其中相邻的 RuBisCOs 主要以三种不同的方式排列：头对头、头对头和并排。最外层的 RuBisCO 沿着外壳有规律地排列，其中大部分直接与外壳相互作用。此外，通过统计分析，我们提出了 RuBisCOs 在β-羧基体中的理想包装模型。这些结果为β-羧酶体的生物发生提供了新的见解，同时也加深了我们对羧酶体高效碳固定功能的理解。

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.

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