Article (Scientific journals)
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.
Virzintiene, Egle; Moparthi, Vamsi K.; Al-Eryani, Yusra et al.
2013In FEBS Letters, 587 (20), p. 3341-7
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Keywords :
Bacillus subtilis/genetics/metabolism; Bacterial Proteins/chemistry/genetics/metabolism; Hydrogen-Ion Concentration; Protein Structure, Tertiary; Complex I; Cytochrome c; Mrp-antiporter complex; MrpA; NuoJ; NuoL
Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Virzintiene, Egle
Moparthi, Vamsi K.
Al-Eryani, Yusra
Shumbe, Léonard ;  Université de Liège - ULiège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Ingénierie des productions végétales et valorisation
Gorecki, Kamil
Hagerhall, Cecilia
Language :
English
Title :
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.
Publication date :
2013
Journal title :
FEBS Letters
ISSN :
0014-5793
eISSN :
1873-3468
Publisher :
Wiley-Blackwell, United States
Volume :
587
Issue :
20
Pages :
3341-7
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Available on ORBi :
since 19 January 2019

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