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NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I

Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on... Full description

Journal Title: FEBS Letters 2011, Vol.585(5), pp.737-743
Main Author: Szklarczyk, Radek
Other Authors: Wanschers, Bas F.J , Nabuurs, Sander B , Nouws, Jessica , Nijtmans, Leo G , Huynen, Martijn A
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2011.01.046
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recordid: elsevier_sdoi_10_1016_j_febslet_2011_01_046
title: NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I
format: Article
creator:
  • Szklarczyk, Radek
  • Wanschers, Bas F.J
  • Nabuurs, Sander B
  • Nouws, Jessica
  • Nijtmans, Leo G
  • Huynen, Martijn A
subjects:
  • Mitochondria
  • Complex I
  • Sequence Conservation
  • Disulfide Bridge
  • Protein Localization
  • Mitochondria
  • Complex I
  • Sequence Conservation
  • Disulfide Bridge
  • Protein Localization
  • Biology
  • Chemistry
  • Anatomy & Physiology
ispartof: FEBS Letters, 2011, Vol.585(5), pp.737-743
description: Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx 9C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I. NDUFA8 and NDUFS3 physically interact by blue native page ( View interaction)
language: eng
source:
identifier: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2011.01.046
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
  • 1873-3468
  • 18733468
url: Link


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titleNDUFB7 and NDUFA8 are located at the intermembrane surface of complex I
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subjectMitochondria ; Complex I ; Sequence Conservation ; Disulfide Bridge ; Protein Localization ; Mitochondria ; Complex I ; Sequence Conservation ; Disulfide Bridge ; Protein Localization ; Biology ; Chemistry ; Anatomy & Physiology
descriptionComplex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx 9C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I. NDUFA8 and NDUFS3 physically interact by blue native page ( View interaction)
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titleNDUFB7 and NDUFA8 are located at the intermembrane surface of complex I
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Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx 9C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I.

NDUFA8 and NDUFS3 physically interact by blue native page ( View interaction)

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Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx 9C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I.

NDUFA8 and NDUFS3 physically interact by blue native page ( View interaction)

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