PMID:15608119

Citation	Korepanova, A, Gao, FP, Hua, Y, Qin, H, Nakamoto, RK and Cross, TA (2005) Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli. Protein Sci. 14:148-58
Abstract	Seventy integral membrane proteins from the Mycobacterium tuberculosis genome have been cloned and expressed in Escherichia coli. A combination of T7 promoter-based vectors with hexa-His affinity tags and BL21 E. coli strains with additional tRNA genes to supplement sparsely used E. coli codons have been most successful. The expressed proteins have a wide range of molecular weights and number of transmembrane helices. Expression of these proteins has been observed in the membrane and insoluble fraction of E. coli cell lysates and, in some cases, in the soluble fraction. The highest expression levels in the membrane fraction were restricted to a narrow range of molecular weights and relatively few transmembrane helices. In contrast, overexpression in insoluble aggregates was distributed over a broad range of molecular weights and number of transmembrane helices.
Links	PubMed PMC2253320 Online version:10.1110/ps.041022305
Keywords	Cloning, Molecular; Escherichia coli/genetics; Escherichia coli/metabolism; Gene Expression Regulation, Bacterial; Intracellular Membranes/metabolism; Membrane Proteins/biosynthesis; Membrane Proteins/genetics; Mycobacterium tuberculosis/genetics
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