Skip to main content
SpringerLink
Log in

Cloning and sequence analysis of the gene encoding 19-kD subunit of Complex I from Dunaliella salina

  • Published:
Molecular Biology Reports Aims and scope Submit manuscript

Abstract

NADH:ubiquinone oxidoreductase (complex I ) of the mitochondrial respiratory chain catalyzes the transfer of electrons from NADH to ubiquinone coupled to proton translocation across the membrane. The cDNA sequence of Dunaliella salina mitochondrial NADH: ubiquinone oxidoreductase 19-kD subunit contains a 682-bp ORF encoding a protein with an apparent molecular mass of 19 kD. The sequence has been submitted to the GenBank database under Accession No. EF566890 (cDNA sequences) and EF566891 (genomic sequence). The deduced amino-acid sequence is 74% identical to Chlamydomonas reinhardtii mitochondrial NADH:ubiquinone oxidoreductase 18-kD subunit. The 19-kD subunit mRNA expression was observed in oxygen deficiency, salt treatment, and rotenone treatment with lower levels. It demonstrate that the 19-kD subunit of Complex I from Dunaliella salina is regulated by these stresses .

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4

Similar content being viewed by others

References

  1. Ramesh H (1998) The 24-kDasubunit of the bovine mitochondrial NADH:ubiquinone oxidoreductase is a G protein. Biochem Biophys Res Commun 244:620–629

    Article  Google Scholar 

  2. Hatefi Y (1985) The mitochondrial electron transport and oxidative phosphorylation system. Annu Rev Biochem 54:1015–1069

    Article  PubMed  CAS  Google Scholar 

  3. Rene C, Paul B, Hubert S et al (1995) Molecular cloning and characterization of the active human mitochondrial NADH:ubiquinone oxidoreductase 24-kDa gene (NDUFV2) and its pseudogene. Genomics 26:461–466

    Article  Google Scholar 

  4. Re´gis S, Pascal M, Vincent P et al (1998) Genomic structure of the human NDUFS8 gene coding for the iron–sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase. Gene 215:1–10

    Article  Google Scholar 

  5. Isabel M, Margarida D, Arnaldo V (2003) The 9.8 kDasubunit of complex I, related to bacterial Na+-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa. J Mol Biol 329:283–290

    Article  CAS  Google Scholar 

  6. Videira A, Duarte M (2002) From NADH to ubiquinone in Neurospora mitochondria. Biochim Biophys Acta 1555:187–191

    Article  PubMed  CAS  Google Scholar 

  7. Yulia V, Bertsova, Alexander V, Bogachev (2004) The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae. FEBS Lett 563:207–212

    Article  CAS  Google Scholar 

  8. Walter K, Julia S, Anja C et al (1999) Na+translocation by the NADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae. Mol Microbiol 33(3):590–598

    Article  Google Scholar 

  9. Matsushita K, Ohnishi T, Kaback H (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26:7732–7737

    Article  PubMed  CAS  Google Scholar 

  10. Yagi T (1991) Bacterial NADH-quinone oxidoreductases. J Bioenerg Biomembr 23:211–225

    Article  PubMed  CAS  Google Scholar 

  11. Hase C, Barquera B (2001) Role of sodium bioenergetics in Vibrio cholerae. Biochim. Biophys Acta 1505:169–178

    Article  PubMed  CAS  Google Scholar 

  12. Barquera B, Hellwig P, Zhou W, Morgan JE, Hase, C et al (2002) Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry 41:3781–3789

    Article  PubMed  CAS  Google Scholar 

  13. Dimroth P (1997) Primary sodium ion translocating enzymes. Biochim Biophys Acta 1318:11–51

    Article  PubMed  CAS  Google Scholar 

  14. Pick U, Karni L, AvronM (1986) Determination of ion content and ion fluxes in the halotolerant alga Dunaliella salina. Plant Physiol 81:92–96

    Article  PubMed  CAS  Google Scholar 

  15. Li G, Liu M, Jiang Y, Qiao DR, Cao Y (2004) Construction and functional gene screening of cDNA library of Dunaliella salina. J Trop Subtrop Bot 12:74–78

    CAS  Google Scholar 

  16. Hare PD, Cress WA, Van Staden J (1998) Dissecting the roles of osmolyte accumulation during stress. Plant Cell Environ 21:535–553

    Article  CAS  Google Scholar 

  17. Noctor G, Foyer CH (1998) Ascorbate and glutathione:keeping active oxygen under control. Annu Rev PlantPhysiol Mol Biol 49:249–279

    Article  CAS  Google Scholar 

  18. McNeil SD, Nuccio ML, Hanson AD (1999) Betaines and related osmoprotectants: targets for metabolic engineering of stress resistance. Plant Physiol 120:945–949

    Article  PubMed  CAS  Google Scholar 

  19. Hamilton III EW, McNaugthon SJ, Coleman JS (2001) Soil Na stress: molecular, physiological and growth responses in Serengeti C4 grasses. Am J Bot 88:1069–1076

    Google Scholar 

  20. Polla BS, Kantengwa S, Francois D, Salvioli S, Franceschi C, Marsac C, Cossarizza A (1996) Mitochondria are selective targets for the protective effects of heat shock against oxidative injury. Proc Natl Acad Sci USA 93:6458–6463

    Article  PubMed  CAS  Google Scholar 

  21. Pobezhimova TP, Voinikov VK, Varakina NN (1997) Thermotolerance and functional stability of particular complexes of the respiratory chain in maize mitochondria incubated in vitro. Russ J Plant Physiol 44:754–758

    Google Scholar 

  22. Yan LJ, Levine RL, Sohal RS (1997) Oxidative damage during aging targets mitochondrial aconitase. Proc Natl Acad Sci USA 94:11168–11172

    Article  PubMed  CAS  Google Scholar 

  23. Downs CA, Heckathorn SA (1998) The mitochondrial small heat-shock protein protects NADH: ubiquinone oxidoreductase of the electron transport chain during heat stress in plants. FEBS Lett 430:246–250

    Article  PubMed  CAS  Google Scholar 

  24. Polyakova L, Vartapetian B (2003) Exogenous nitrate as a terminal acceptor of electrons in rice (Oryza sativa) coleoptiles and wheat (Triticum aestivum) roots under strict anoxia. Russ J Plant Physiol 50:808–812

    Article  CAS  Google Scholar 

  25. Boris B, Vartapetian, Michael B, Jackson (1997) Plant adaptations to anaerobic stress. Ann Bot 79(Supplement A):3–20

    Google Scholar 

  26. Mary A, Tichi, Wim G, Meijer F, Robert T (2001) Complex I and its involvement in redox homeostasis and carbon and nitrogen metabolism in Rhodobacter capsulatus. J Bacteriol 183:7285–7294

    Article  CAS  Google Scholar 

  27. Boyer JS (1982) Plant productivity and environment. Science 218:443–448

    Article  PubMed  Google Scholar 

  28. William H, Scott H (2001) Mitochondrial adaptations to NaCl complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine. Plant Physiol 126:1266–1274

    Article  Google Scholar 

  29. Yidong B, Giuseppe A (1998) The mtDNA-encoded ND6subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme. EMBO J 17(16):4848–4858

    Article  Google Scholar 

  30. Jing F, Yudong W, Diana S (2001) Isolation and characterization of complex I, rotenone-sensitive NADH:ubiquinone oxidoreductase, from the procyclic forms of Trypanosoma brucei. Eur. J. Biochem 268:3075–3082

    Article  Google Scholar 

  31. Johannes A, Ian A (2006) Benzothiadiazole inhibits mitochondrial NADH:ubiquinone oxidoreductase in tobacco. J Plant Physiol 163:877–882

    Article  CAS  Google Scholar 

  32. Nianyu L, Kathy R, Gretchen L, Jennie S, Bartek R (2003) Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J Biol Chem 278(10):8516–8525

    Article  CAS  Google Scholar 

Download references

Acknowledgements

This work was supported by the National Natural Science Foundation of China (30470928, 30270711, 30500287).

Author information

Authors and Affiliations

  1. Key Laboratory of bio-resources and Eco-environment, Ministry of Education, College of Life Sciences, Sichuan University, Sichuan, P.R. China

    Yi Liu, Dai Rong Qiao, Hong Bo Zheng, Xu Lan Dai, Lin Han Bai, Jing Zeng & Yi Cao

  2. Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, 610064, P.R. China

    Yi Liu, Dai Rong Qiao, Hong Bo Zheng, Xu Lan Dai, Lin Han Bai, Jing Zeng & Yi Cao

Authors
  1. Yi Liu
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Dai Rong Qiao
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Hong Bo Zheng
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Xu Lan Dai
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Lin Han Bai
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Jing Zeng
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Yi Cao
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Yi Cao.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Liu, Y., Qiao, D.R., Zheng, H.B. et al. Cloning and sequence analysis of the gene encoding 19-kD subunit of Complex I from Dunaliella salina . Mol Biol Rep 35, 397–403 (2008). https://doi.org/10.1007/s11033-007-9099-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11033-007-9099-x

Keywords

Search

Navigation