Advances in Understanding Carboxysome Assembly in Prochlorococcus and Synechococcus Implicate CsoS2 as a Critical Component

Life

Fei Cai¹  Zhicheng Dou⁵  Susan L. Bernstein¹  Ryan Leverenz³  Eric B. Williams⁵  Sabine Heinhorst⁵  Jessup Shively²  Gordon C. Cannon⁵  Cheryl A. Kerfeld¹  John C. Meeks⁴ 

[1] Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA; E-Mails:;Department of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA; E-Mail:;MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA; E-Mail:Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA;;Department of Chemistry and Biochemistry, The University of Southern Mississippi, Hattiesburg, MS 39406-5043, USA; E-Mails:

关键词: CO₂ concentrating mechanism (CCM);    carboxysome;    RuBisCO;    CsoS2;    assembly;    intrinsically disordered protein;    peptide array;   

DOI  :  10.3390/life5021141

来源: mdpi

【 摘 要 】

The marine Synechococcus and Prochlorococcus are the numerically dominant cyanobacteria in the ocean and important in global carbon fixation. They have evolved a CO₂-concentrating-mechanism, of which the central component is the carboxysome, a self-assembling proteinaceous organelle. Two types of carboxysome, α and β, encapsulating form IA and form IB d-ribulose-1,5-bisphosphate carboxylase/oxygenase, respectively, differ in gene organization and associated proteins. In contrast to the β-carboxysome, the assembly process of the α-carboxysome is enigmatic. Moreover, an absolutely conserved α-carboxysome protein, CsoS2, is of unknown function and has proven recalcitrant to crystallization. Here, we present studies on the CsoS2 protein in three model organisms and show that CsoS2 is vital for α-carboxysome biogenesis. The primary structure of CsoS2 appears tripartite, composed of an N-terminal, middle (M)-, and C-terminal region. Repetitive motifs can be identified in the N- and M-regions. Multiple lines of evidence suggest CsoS2 is highly flexible, possibly an intrinsically disordered protein. Based on our results from bioinformatic, biophysical, genetic and biochemical approaches, including peptide array scanning for protein-protein interactions, we propose a model for CsoS2 function and its spatial location in the α-carboxysome. Analogies between the pathway for β-carboxysome biogenesis and our model for α-carboxysome assembly are discussed.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.