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Deciphering molecular details in the assembly of alpha-type carboxysome.

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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Liu Y,He X,Lim W,Mueller J,Lawrie J,Kramer L,Guo J,Niu W

doi

10.1038/s41598-018-33074-x

subject

Has Abstract

pub_date

2018-10-10 00:00:00

pages

15062

issue

1

issn

2045-2322

pii

10.1038/s41598-018-33074-x

journal_volume

8

pub_type

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