Conserved and repetitive motifs in an intrinsically disordered protein drive ⍺-carboxysome assembly.

ABSTRACT: All cyanobacteria and some chemoautotrophic bacteria fix CO₂ into sugars using specialized proteinaceous compartments called carboxysomes. Carboxysomes enclose the enzymes Rubisco and carbonic anhydrase inside a layer of shell proteins to increase the CO₂ concentration for efficient carbon fixation by Rubisco. In the ⍺-carboxysome lineage, a disordered and highly repetitive protein named CsoS2 is essential for carboxysome formation and function. Without it, the bacteria require high CO₂ to grow. How does a protein predicted to be lacking structure serve as the architectural scaffold for such a vital cellular compartment? In this study, we identify key residues present in the repeats of CsoS2, VTG and Y, which are necessary for building functional ⍺-carboxys

SUBMITTER: Turnsek JB 

PROVIDER: S-EPMC11365436 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature