Publication: Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation
Issued Date
2020-03-01
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ISSN
15459985
15459993
15459993
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2-s2.0-85081570409
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Mahidol University
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SCOPUS
Bibliographic Citation
Nature Structural and Molecular Biology. Vol.27, No.3 (2020), 281-287
Suggested Citation
Luke M. Oltrogge, Thawatchai Chaijarasphong, Allen W. Chen, Eric R. Bolin, Susan Marqusee, David F. Savage Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. Nature Structural and Molecular Biology. Vol.27, No.3 (2020), 281-287. doi:10.1038/s41594-020-0387-7 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/53573
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Title
Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation
Abstract
© 2020, The Author(s), under exclusive licence to Springer Nature America, Inc. 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.