期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 27, 期 3, 页码 281-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41594-020-0387-7
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资金
- University of California Office of the President, Multicampus Research Programs and Initiatives [MR-15-328599]
- National Institutes of Health [R01 GM124149, P30 GM124169]
- US Department of Energy [DE-SC00016240]
- National Institute of General Medical Sciences [R01GM129241, R01GM050945]
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 alpha-carboxysome, there is little molecular insight into protein-protein interactions that drive the assembly process. Here, studies on the alpha-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 alpha-carboxysome formation. Structural and binding studies show that a repeated peptide motif in the N-terminal domain of CsoS2 mediates multivalent interactions with assembled Rubisco to facilitate its encapsulation into the carboxysome.
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