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Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation.
Nature Structural & Molecular Biology ( IF 12.5 ) Pub Date : 2020-03-02 , DOI: 10.1038/s41594-020-0387-7
Luke M Oltrogge 1 , Thawatchai Chaijarasphong 1, 2 , Allen W Chen 3 , Eric R Bolin 4, 5 , Susan Marqusee 1, 3, 5 , David F Savage 1
Affiliation  

Carboxysomes are bacterial microcompartments that function as the centerpiece of the bacterial CO2-concentrating mechanism by facilitating high CO2 concentrations near the carboxylase Rubisco. The carboxysome self-assembles from thousands of individual proteins into icosahedral-like particles with a dense enzyme cargo encapsulated within a proteinaceous shell. In the case of the α-carboxysome, there is little molecular insight into protein-protein interactions that drive the assembly process. Here, studies on the α-carboxysome from Halothiobacillus neapolitanus demonstrate that Rubisco interacts with the N terminus of CsoS2, a multivalent, intrinsically disordered protein. X-ray structural analysis of the CsoS2 interaction motif bound to Rubisco reveals a series of conserved electrostatic interactions that are only made with properly assembled hexadecameric Rubisco. Although biophysical measurements indicate that this single interaction is weak, its implicit multivalency induces high-affinity binding through avidity. Taken together, our results indicate that CsoS2 acts as an interaction hub to condense Rubisco and enable efficient α-carboxysome formation.

中文翻译:

CsoS2和Rubisco之间的多价相互作用介导了α-羧基体的形成。

羧化物是细菌微隔室,其通过促进羧化酶Rubisco附近的高CO2浓度而充当细菌CO2浓缩机制的核心。羧化酶将数千种蛋白质自组装成二十面体状颗粒,并在蛋白质壳中包裹着稠密的酶货物。就α-羧基体而言,对驱动组装过程的蛋白质-蛋白质相互作用的分子了解很少。在这里,对来自那不勒斯硫杆菌的α-羧基体的研究表明,Rubisco与CsoS2的N末端相互作用,CsoS2是一种多价的,内在无序的蛋白质。对与Rubisco结合的CsoS2相互作用基序的X射线结构分析揭示了一系列保守的静电相互作用,这些相互作用只有通过正确组装的十六进制Rubisco才能完成。尽管生物物理测量表明该单一相互作用较弱,但其隐性多价通过亲和力诱导了高亲和力结合。两者合计,我们的结果表明CsoS2充当相互作用枢纽,以浓缩Rubisco并实现有效的α-羧基体形成。
更新日期:2020-03-02
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