The Repertoire and Evolution of ATP-Binding Cassette Systems in <Emphasis Type="Italic">Synechococcus</Emphasis> and <Emphasis Type="Italic">Prochlorococcus</Emphasis> |
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Authors: | Lijing Bu Jian Xiao Lijun Lu Gang Xu Jinsong Li Fangqing Zhao Xiaokun Li Jinyu Wu |
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Institution: | (1) Zhejiang Provincial Key Laboratory of Medical Genetics, Institute of Biomedical Informatics, Wenzhou Medical College, Wenzhou, 325000, China;(2) Zhejiang Provincial Key Laboratory of Biotechnology Pharmaceutical Engineering, School of Pharmaceutical Science, Wenzhou Medical College, Wenzhou, 325000, China;(3) Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA; |
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Abstract: | 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
B12 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. |
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