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.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4066114
- author
- Virzintiene, Egle LU ; Moparthi, Vamsi LU ; Al-Eryani, Yusra LU ; Shumbe, Leonard ; Gorecki, Kamil LU and Hägerhäll, Cecilia LU
- organization
- publishing date
- 2013
- 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
- pmid:24021651
- 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
- 2016-04-01 09:49:20
- date last changed
- 2022-01-25 17:01:24
@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}}, doi = {{10.1016/j.febslet.2013.08.027}}, volume = {{587}}, year = {{2013}}, }