title: Analysis of Streptomyces coelicolor membrane proteome using two-dimensional native/native and native/sodium dodecyl sulfate gel electrophoresis.
abstract: Analysis of the oligomeric state of a protein may provide insights into its physiological functions. Because membrane proteins are considered to be the workhorses of energy generation and polypeptide and nutrient transportation, in this study we characterized the membrane-associated proteome of Streptomyces coelicolor by two-dimensional (2D) blue native/sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), high-resolution clear native/native PAGE, and native/SDS-PAGE. A total of 77 proteins were identified, and 20 proteins belonging to 15 complexes were characterized. Moreover, the resolution of high-resolution clear native/SDS-PAGE is much higher than that of blue native/SDS-PAGE. OBP (SCO5477) and BldKB (SCO5113) were identified as the main protein spots from the membrane fractions of S. coelicolor M145, suggesting that these two proteins are involved in extracellular peptide transportation. These two transporters exhibited multiple oligomeric states in the native PAGE system, which may suggest their multiple physiological functions in the development of S. coelicolor.
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China; School of Marine Science and Technology, Jiangsu Marine Resources Development Research Institute, Huaihai Institute of Technology, Lianyungang, Jiangsu Province 222005, People's Republic of China.
authors.forename: Fuhou
authors.initials: F
authors.lastname: Li
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China.
authors.forename: Jingdan
authors.initials: J
authors.lastname: Liang
authors.affiliation: School of Marine Science and Technology, Jiangsu Marine Resources Development Research Institute, Huaihai Institute of Technology, Lianyungang, Jiangsu Province 222005, People's Republic of China.
authors.forename: Weixia
authors.initials: W
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China.
authors.forename: Xiufen
authors.initials: X
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China. Electronic address: zxdeng@sjtu.edu.cn.
authors.forename: Zixin
authors.initials: Z
authors.lastname: Deng
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China. Electronic address: wangzhijun@sjtu.edu.cn.
authors.forename: Zhijun
authors.initials: Z
authors.lastname: Wang
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000378:metabolism*; D020543:Proteome / Q000378:metabolism*; D048372:Streptomyces coelicolor / Q000378:metabolism*; D057825:Two-Dimensional Difference Gel Electrophoresis
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D020543:Proteome
keywords: Blue native electrophoresis; High-resolution clear native electrophoresis; Membrane proteome; Streptomyces coelicolor