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Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters

Mathiesen, Cecilie LU and Hägerhäll, Cecilia LU (2002) In Biochimica et Biophysica Acta - Bioenergetics 1556(2-3). p.121-132
Abstract
Nicotinamide adenine dinucleotide-reduced form (NADH):quinone oxidoreductase (respiratory Complex I), F420H2 oxidoreductase and complex, membrane-bound NiFe-hydrogenase contain protein subunits homologous to a certain type of bona fide antiporters. In Complex I, these polypeptides (NuoL/ND5, NuoM/ND4, NuoN/ND2) are most likely core components of the proton pumping mechanism, and it is thus important to learn more about their structure and function. In this work, we have determined the transmembrane topology of one such polypeptide, and built a 2D structural model of the protein valid for all the homologous polypeptides. The experimentally determined transmembrane topology was different from that predicted by majority vote hydrophobicity... (More)
Nicotinamide adenine dinucleotide-reduced form (NADH):quinone oxidoreductase (respiratory Complex I), F420H2 oxidoreductase and complex, membrane-bound NiFe-hydrogenase contain protein subunits homologous to a certain type of bona fide antiporters. In Complex I, these polypeptides (NuoL/ND5, NuoM/ND4, NuoN/ND2) are most likely core components of the proton pumping mechanism, and it is thus important to learn more about their structure and function. In this work, we have determined the transmembrane topology of one such polypeptide, and built a 2D structural model of the protein valid for all the homologous polypeptides. The experimentally determined transmembrane topology was different from that predicted by majority vote hydrophobicity analyses of members of the superfamily. A detailed phylogenetic analysis of a large set of primary sequences shed light on the functional relatedness of these polypeptides. (Less)
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type
Contribution to journal
publication status
published
subject
keywords
Fusion protein, NADH:quinone oxidoreductase, F420H2 oxidoreductase, NiFe-hydrogenase, Antiporter, Alkaline phosphatase
in
Biochimica et Biophysica Acta - Bioenergetics
volume
1556
issue
2-3
pages
121 - 132
publisher
Elsevier
external identifiers
  • pmid:12460669
  • wos:000179691200006
  • scopus:0037010862
ISSN
0005-2728
DOI
10.1016/S0005-2728(02)00343-2
language
English
LU publication?
yes
id
9b98e449-ff7e-4192-994c-9d72b1c3682b (old id 124858)
date added to LUP
2016-04-01 16:51:51
date last changed
2022-04-23 01:05:46
@article{9b98e449-ff7e-4192-994c-9d72b1c3682b,
  abstract     = {{Nicotinamide adenine dinucleotide-reduced form (NADH):quinone oxidoreductase (respiratory Complex I), F420H2 oxidoreductase and complex, membrane-bound NiFe-hydrogenase contain protein subunits homologous to a certain type of bona fide antiporters. In Complex I, these polypeptides (NuoL/ND5, NuoM/ND4, NuoN/ND2) are most likely core components of the proton pumping mechanism, and it is thus important to learn more about their structure and function. In this work, we have determined the transmembrane topology of one such polypeptide, and built a 2D structural model of the protein valid for all the homologous polypeptides. The experimentally determined transmembrane topology was different from that predicted by majority vote hydrophobicity analyses of members of the superfamily. A detailed phylogenetic analysis of a large set of primary sequences shed light on the functional relatedness of these polypeptides.}},
  author       = {{Mathiesen, Cecilie and Hägerhäll, Cecilia}},
  issn         = {{0005-2728}},
  keywords     = {{Fusion protein; NADH:quinone oxidoreductase; F420H2 oxidoreductase; NiFe-hydrogenase; Antiporter; Alkaline phosphatase}},
  language     = {{eng}},
  number       = {{2-3}},
  pages        = {{121--132}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta - Bioenergetics}},
  title        = {{Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters}},
  url          = {{http://dx.doi.org/10.1016/S0005-2728(02)00343-2}},
  doi          = {{10.1016/S0005-2728(02)00343-2}},
  volume       = {{1556}},
  year         = {{2002}},
}