Structure and function of the C-terminal domain of MrpA in the Bacillus subtilis Mrp-antiporter complex - The evolutionary progenitor of the long horizontal helix in complex i

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Abstract

MrpA and MrpD are homologous to NuoL, NuoM and NuoN in complex I over the first 14 transmembrane helices. In this work, the C-terminal domain of MrpA, outside this conserved area, was investigated. The transmembrane orientation was found to correspond to that of NuoJ in complex I. We have previously demonstrated that the subunit NuoK is homologous to MrpC. The function of the MrpA C-terminus was tested by expression in a previously used Bacillus subtilis model system. At neutral pH, the truncated MrpA still worked, but at pH 8.4, where Mrp-complex formation is needed for function, the C-terminal domain of MrpA was absolutely required. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Virzintiene, E., Moparthi, V. K., Al-Eryani, Y., Shumbe, L., Górecki, K., & Hägerhäll, C. (2013). Structure and function of the C-terminal domain of MrpA in the Bacillus subtilis Mrp-antiporter complex - The evolutionary progenitor of the long horizontal helix in complex i. FEBS Letters, 587(20), 3341–3347. https://doi.org/10.1016/j.febslet.2013.08.027

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