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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.

Virzintiene, Egle LU ; Moparthi, Vamsi LU ; Al-Eryani, Yusra LU ; Shumbe, Leonard; Gorecki, Kamil LU and Hägerhäll, Cecilia LU (2013) In FEBS Letters 587(20). p.3341-3347
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
587
issue
20
pages
3341 - 3347
publisher
Wiley-Blackwell
external identifiers
  • wos:000325078600009
  • pmid:24021651
  • scopus:84884909250
ISSN
1873-3468
DOI
10.1016/j.febslet.2013.08.027
language
English
LU publication?
yes
id
d8432f55-c192-4588-9d3c-6f17df64e662 (old id 4066114)
date added to LUP
2013-11-14 11:16:48
date last changed
2019-02-20 01:03:11
@article{d8432f55-c192-4588-9d3c-6f17df64e662,
  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.},
  author       = {Virzintiene, Egle and Moparthi, Vamsi and Al-Eryani, Yusra and Shumbe, Leonard and Gorecki, Kamil and Hägerhäll, Cecilia},
  issn         = {1873-3468},
  language     = {eng},
  number       = {20},
  pages        = {3341--3347},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  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.},
  url          = {http://dx.doi.org/10.1016/j.febslet.2013.08.027},
  volume       = {587},
  year         = {2013},
}