Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly

Journal article

Abstract Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal “molecular thread” stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications

Authors: Ni, T; Jiang, Q; Ng, PC; Shen, J; Dou, H

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Nature Research
• Journal: Nature Communications
• Volume: 14
• Issue: 1
• Pages: 5512-5512
• Article number: 5512
• Publication date: 2023-09-07
• DOI: 10.1038/s41467-023-41211-y
• EISSN: 2041-1723
• ISSN: 2041-1723
• Language: English
• Keywords: Thread (computing); Biophysics; Biology; Computer science; Nanotechnology; Enzyme; Chemistry; Organelle; Materials science; RuBisCO; Computational biology; Biochemistry