ArticleScientific reports2018
Deciphering molecular details in the assembly of alpha-type carboxysome.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles.ACS nano · 2025Article
- Review
- Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly.Nature communications · 2023Article
- Probing the Internal pH and Permeability of a Carboxysome Shell.Biomacromolecules · 2022Article
- Incorporation of Functional Rubisco Activases into Engineered Carboxysomes to Enhance Carbon Fixation.ACS synthetic biology · 2022Article
- Complex structure reveals CcmM and CcmN form a heterotrimeric adaptor in β-carboxysome.Protein science : a publication of the Protein Society · 2021Article
- Review
- Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021Review
- Prospects for Engineering Biophysical COAnnual review of plant biology · 2020Review
- Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation.Nature structural & molecular biology · 2020Article
- Hybrid Cyanobacterial-Tobacco Rubisco Supports Autotrophic Growth and Procarboxysomal Aggregation.Plant physiology · 2020Article
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Bacterial microcompartments: catalysis-enhancing metabolic modules for next generation metabolic and biomedical engineering.BMC biology · 2019Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Bacterial microcompartments (BMCs) are promising natural protein structures for applications that require the segregation of certain metabolic functions or molecular species in a defined microenvironment. To understand how endogenous cargos are packaged inside the protein shell is key for using BMCs as nano-scale reactors or delivery vesicles. In this report, we studied the encapsulation of RuBisCO into the α-type carboxysome from Halothiobacillus neapolitan. Our experimental data revealed that the CsoS2 scaffold proteins engage RuBisCO enzyme through an interaction with the small subunit (CbbS). In addition, the N domain of the large subunit (CbbL) of RuBisCO interacts with all shell proteins that can form the hexamers. The binding affinity between the N domain of CbbL and one of the major shell proteins, CsoS1C, is within the submicromolar range. The absence of the N domain also prevented the encapsulation of the rest of the RuBisCO subunits. Our findings complete the picture of how RuBisCOs are encapsulated into the α-type carboxysome and provide insights for future studies and engineering of carboxysome as a protein shell.
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Registered trials
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