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- W2153284235 abstract "Abstract Overproduction of membrane proteins can be a cumbersome task, particularly if high yields are desirable. NADH:quinone oxidoreductase (Complex I) contains several very large membrane‐spanning protein subunits that hitherto have been impossible to express individually in any appreciable amounts in Escherichia coli . The polypeptides contain no prosthetic groups and are poorly antigenic, making optimization of protein production a challenging task. In this work, the C‐terminal ends of the Complex I subunits NuoH, NuoL, NuoM, and NuoN from E. coli Complex I and the bona fide antiporters MrpA and MrpD were genetically fused to the cytochrome c domain of Bacillus subtilis cytochrome c 550 . Compared with other available fusion‐protein tagging systems, the cytochrome c has several advantages. The heme is covalently bound, renders the proteins visible by optical spectroscopy, and can be used to monitor, quantify, and determine the orientation of the polypeptides in a plethora of experiments. For the antiporter‐like subunits NuoL, NuoM, and NuoN and the real antiporters MrpA and MrpD, unprecedented amounts of holo‐cytochrome fusion proteins could be obtained in E. coli . The NuoHcyt polypeptide was also efficiently produced, but heme insertion was less effective in this construct. The cytochrome c 550 domain in all the fusion proteins exhibited normal spectra and redox properties, with an E m of about +170 mV. The MrpA and MrpD antiporters remained functional after being fused to the cytochrome c ‐tag. Finally, a his‐tag could be added to the cytochrome domain, without any perturbations to the cytochrome properties, allowing efficient purification of the overexpressed fusion proteins." @default.
- W2153284235 created "2016-06-24" @default.
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- W2153284235 date "2010-07-21" @default.
- W2153284235 modified "2023-10-18" @default.
- W2153284235 title "A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli-Expression and characterization of cytochrome-tagged Complex I subunits" @default.
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- W2153284235 doi "https://doi.org/10.1002/pro.424" @default.
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