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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
Author(s) -
Virzintiene Egle,
Moparthi Vamsi K.,
Al-Eryani Yusra,
Shumbe Leonard,
Górecki Kamil,
Hägerhäll Cecilia
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.08.027
Subject(s) - bacillus subtilis , transmembrane domain , transmembrane protein , function (biology) , biochemistry , protein subunit , helix (gastropod) , homologous chromosome , antiporter , domain (mathematical analysis) , chemistry , biology , microbiology and biotechnology , amino acid , bacteria , genetics , receptor , membrane , gene , ecology , mathematical analysis , mathematics , snail
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.