The repertoire and evolution of ATP-binding cassette systems in Synechococcus and Prochlorococcus

Synechococcus and Prochlorococcus have made great contributions to earth's photosynthetic biomass. ATP-binding cassette (ABC) protein systems have been characterized to play important roles in various physiological functions, including carbon fixation, phosphate assimilation, and vitamin B(12) metabolism. In this study, the repertoire and domain architectures of ABC systems in Synechococcus and Prochlorococcus, as well as their potential evolutionary mechanism, have been surveyed extensively. Comparative analysis revealed an uneven phylogenetic distribution of the ABC systems in these organisms, and in particular that fresh-water Synechococcus strains contain more ABC systems than those of marine ones. Phylogenetic analysis indicated that lineage-specific gene expansion and duplication may be the important forces driving the variability of ABC systems in fresh-water Synechococcus and such an expansion was likely to be relevant to their ecological tolerance. At the domain level, ATP-binding domains in several ABC systems were found to fuse with many additional domains after the divergence from their common ancestor, indicating the versatile functions of ABC systems in cyanobacteria. Subsequently, 19 ABC system families were deduced to be the core set of ABC systems conserved in all marine-living Synechococcus and Prochlorococcus. In conclusion, the comprehensive survey of ABC systems in Synechococcus and Prochlorococcus provides novel insights into their potential evolutionary mechanism and the basis for further investigation of their physiological roles.