PMID:10544236

Citation	Bungert, S, Krafft, B, Schlesinger, R and Friedrich, T (1999) One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography. FEBS Lett. 460:207-11
Abstract	The proton-pumping NADH:ubiquinone oxidoreductase, also called complex I, is the first energy-transducing complex of many respiratory chains. Complex I of Escherichia coli can be split into three fragments. One of these fragments, the soluble NADH dehydrogenase fragment, represents the electron input part of complex I. It comprises the subunits NuoE, F and G and harbors one flavin mononucleotide and up to six iron-sulfur clusters. Here, we report the one-step purification of this fragment by means of affinity chromatography on StrepTactin. This was achieved by fusing the Strep-tag II peptide to the C-terminus of NuoF or NuoG. Fusion of this peptide to the N-terminus of either NuoE or NuoF disturbed the assembly of the NADH dehydrogenase fragment.
Links	PubMed
Keywords	Base Sequence; Chromatography, Affinity/methods; DNA Primers/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Molecular Sequence Data; NAD(P)H Dehydrogenase (Quinone)/isolation & purification; NADH Dehydrogenase/isolation & purification; Plasmids/metabolism; Recombinant Fusion Proteins/metabolism; Streptavidin/chemistry
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