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Gene Review

Tb10.6k15.0960  -  NADH dehydrogenase

Trypanosoma brucei brucei TREU927

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High impact information on Tb10.6k15.0960

  • Steady-state levels of unedited ND9 transcripts are greater in bloodstream than in procyclic forms, but edited ND9 mRNA is present in similar abundance in both life cycle stages [1].
  • This protein contains two iron-sulfur cysteine motifs and is homologous to a subunit of NADH dehydrogenase and to other electron-carrier proteins [2].
  • The production of fermentative products seems to be due to a relative inefficiency of the respiratory chain, which lacks NADH dehydrogenase and the first phosphorylation site and preferentially uses succinate as substrate [3].
  • Limited amino acid sequence and hydrophobicity profile similarities suggest that the protein encoded by edited CR5 mRNA may be a subunit of NADH dehydrogenase [4].
  • Hypotonic treatment of intact mitochondria revealed that the NADH dehydrogenase is located in the inner membrane/matrix fraction facing the matrix [5].

Biological context of Tb10.6k15.0960

  • Sequence comparisons indicate that its 5' terminus is the homologue of the downstream portion of the NADH dehydrogenase subunit 7 gene and that its 3' region is homologous to the maxicircle unidentified reading frame II gene [6].
  • Consequently, NADH dehydrogenase, site I of oxidative phosphorylation, is the source of the EMF and the plant-like trypanosome alternative oxidase (TAO) supports the electron flow serving as the terminal oxidase of the chain [7].
  • The other (844 nt, located between 1.7 and 2.55 kb downstream of the NADH-dehydrogenase subunit 5 gene) contains arrays of repetitive sequences which are also found outside this area [8].

Associations of Tb10.6k15.0960 with chemical compounds


Other interactions of Tb10.6k15.0960

  • The presence of three subunits of NADH dehydrogenase was observed in immunoblots of mitochondrial proteins with specific antibodies raised against peptides corresponding to predicted antigenic regions of these proteins, which provides further evidence for the presence of NADH dehydrogenase [9].


  1. Extensive editing of CR2 maxicircle transcripts of Trypanosoma brucei predicts a protein with homology to a subunit of NADH dehydrogenase. Souza, A.E., Shu, H.H., Read, L.K., Myler, P.J., Stuart, K.D. Mol. Cell. Biol. (1993) [Pubmed]
  2. Maxicircle CR1 transcripts of Trypanosoma brucei are edited and developmentally regulated and encode a putative iron-sulfur protein homologous to an NADH dehydrogenase subunit. Souza, A.E., Myler, P.J., Stuart, K. Mol. Cell. Biol. (1992) [Pubmed]
  3. Aerobic fermentation of glucose by trypanosomatids. Cazzulo, J.J. FASEB J. (1992) [Pubmed]
  4. Editing of Trypanosoma brucei maxicircle CR5 mRNA generates variable carboxy terminal predicted protein sequences. Read, L.K., Wilson, K.D., Myler, P.J., Stuart, K. Nucleic Acids Res. (1994) [Pubmed]
  5. Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization. Fang, J., Beattie, D.S. Biochemistry (2002) [Pubmed]
  6. Maxicircle genomic organization and editing of an ATPase subunit 6 RNA in Trypanosoma cruzi. Ochs, D.E., Otsu, K., Teixeira, S.M., Moser, D.R., Kirchhoff, L.V. Mol. Biochem. Parasitol. (1996) [Pubmed]
  7. Mitochondrial development in Trypanosoma brucei brucei transitional bloodstream forms. Bienen, E.J., Saric, M., Pollakis, G., Grady, R.W., Clarkson, A.B. Mol. Biochem. Parasitol. (1991) [Pubmed]
  8. The variable region of the Trypanosoma brucei kinetoplast maxicircle: sequence and transcript analysis of a repetitive and a non-repetitive fragment. de Vries, B.F., Mulder, E., Brakenhoff, J.P., Sloof, P., Benne, R. Mol. Biochem. Parasitol. (1988) [Pubmed]
  9. The presence of rotenone-sensitive NADH dehydrogenase in the long slender bloodstream and the procyclic forms of Trypanosoma brucei brucei. Beattie, D.S., Howton, M.M. Eur. J. Biochem. (1996) [Pubmed]
  10. Rotenone-insensitive NADH dehydrogenase is a potential source of superoxide in procyclic Trypanosoma brucei mitochondria. Fang, J., Beattie, D.S. Mol. Biochem. Parasitol. (2002) [Pubmed]
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