Advertisement

Phosphorylation Level of Complex V Proteins of Higher Plant Mitochondria Correlates with Their Redox State

  • I. Yu. SubotaEmail author
  • M. V. Koulintchenko
  • A. Sh. Arziev
  • Yu. M. Konstantinov
ARTICLES

Abstract

The effect of synthetic cytokinin BAP (6-benzylaminopurine) on protein phosphorylation in isolated maize mitochondria was investigated. The effect of BAP in comparison with classical inhibitors of the mitochondria respiratory complexes, such as rotenone, malonate, SHAM, and KCN on the level of mitochondrial protein phosphorylation was studied. Assessment of the activity of respiratory complexes I and II by the BN-PAGE (blue native polyacrylamide gel electrophoresis) in mitochondria untreated and treated with BAP has not revealed any difference in the activity of these complexes. Investigation of the mitochondrial complex V activity under BAP treatment has shown a significant decrease in the mitochondrial ATPase activity. The effect of BAP was similar to the effect of such a specific inhibitor of the membrane-bound mitochondrial ATPase as oligomycin and an inhibitor of protein tyrosine kinases genistein.

Keywords:

Zea mays mitochondria phosphorylation/dephosphorylation of proteins respiratory complexes cytokinins 6-benzylaminopurine genistein 

Notes

ACKNOWLEDGMENTS

The work was performed using the equipment of the CSU Bioanalytics of the Siberian Institute of plant physiology and biochemistry SB RAS (Irkutsk).

COMPLIANCE WITH ETHICAL STANDARDS

The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.

REFERENCES

  1. 1.
    Goldental M.J., Marin-Garcia J. 2004. Mitochondrial signaling pathways: A receiver/integrator organello. Mol. Cell. Biochem. 262, 1–16.CrossRefGoogle Scholar
  2. 2.
    Pagliarini D.J., Dixon J.E. 2006. Mitochondrial modu-lation: Reversible phosphorylation takes center stage? TRENDS Biochem. Sci. 31, 26–34.CrossRefGoogle Scholar
  3. 3.
    Hughes W.A., Halestrap A.P. 1981. The regulation of branched-chain 2-oxo acid dehydrogenase of liver, kidney and heart by phosphorylation. Biochem. J. 196, 459–469.CrossRefGoogle Scholar
  4. 4.
    Millar A.H., Sweetlove I.J., Giege P., Leaver C.J. 2001. Analysis of the Arabidopsis mitochondrial proteome. Plant. Physiol. 127, 1711–1727.CrossRefGoogle Scholar
  5. 5.
    Havelund J.F., Thelen J.J., Moller I.M. 2013. Biochemistry, proteomics and phosphoproteomic of plant mitochondria from non-photosynthetic cell. Plant Sci. 4, 1–10.Google Scholar
  6. 6.
    Hepler P.K. 2005. Calcium: A central regulator of plant growth and development. Plant Cell. 17, 2142–2155.CrossRefGoogle Scholar
  7. 7.
    Chauveau M., Dizengremel P., Roussux J. 1983. Interaction of benzylaminopurine with electron transport in plant mitochondria during malate oxidation. Physiol. Plant. 73, 945–948.CrossRefGoogle Scholar
  8. 8.
    Subota I.Yu., Arziev A.Sh., Konstantinov Yu.M. 2004. The involvement of protein phosphorylation/ dephosphorylation in the redox control of translation in cereal mitochondria. Rus. J. Plant Physiol. 51 (6), 872–877.CrossRefGoogle Scholar
  9. 9.
    Subota I.Yu., Arziev A.Sh., Koulintchenko M.V., Konstantinov Yu.M. 2013. Ca2+ ions modulate the level of phosphorylation/dephosphorylation of mitochondrial proteins. Biol. Membrany (Rus.). 30 (3), 230–237.Google Scholar
  10. 10.
    Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature. 277, 174–182.Google Scholar
  11. 11.
    Timmons T.M., Dunbar B.S. 1990. Protein blotting and immunodetection Meth. Enzymol. 18, 679–701.CrossRefGoogle Scholar
  12. 12.
    Heinemeyer J., Lewejohann D., Braun H.P. 2007. Blue-native gel electrophoresis for the characterization of protein complexes in plants. Methods Mol. Biol. 355, 343–352.Google Scholar
  13. 13.
    Sabar M., Balk J., Leaver C.J. 2005. Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis. Plant J. 44, 893–901.CrossRefGoogle Scholar
  14. 14.
    Zheng J., Ramires V.D. 1993. Rapid inhibition of rat brain mitochondria proton F0F1-ATPase by estrogens: Comparison with Na+,K+-ATPase of porcine cortex. Eur. J. Pharmacol. 368, 92–102.Google Scholar
  15. 15.
    Salgado I., Oliveira H.C. 2015. The role of alternative respiratory protein in nitric oxide metabolism by plant mitochondria. In: Alternative respiratory pathway in higher plants. Eds. Kapuganti J.G. Hoboken, New Jersey: Wiley Blackwell, p. 95–100.Google Scholar
  16. 16.
    Muraoka S., Slater E.C. 1969. The redox states of respiratory chain components in rat liver mitochondria. Biochim. Biophys. Acta. 180, 221–226.CrossRefGoogle Scholar
  17. 17.
    Konstantinov Y.M., Lutsenko G.M., Podsossonny V.A. 1995. Genetic functions of isolated maize mitochondria under model changes of redox conditions. Biochem. Mol. Biol. Int. 36, 319–326.Google Scholar
  18. 18.
    Brineger C., Shan G., Cooper G. 1996. Photoaffinity labelling of cytokinin-binding integral membrane protein in plant mitochondria. In: Plant Gormone Signal Perception and Transduction. Eds Smith A.R. Dordrecht, Netherlands: Kluwer Acad. Publ., p. 83–88.Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2019

Authors and Affiliations

  • I. Yu. Subota
    • 1
    Email author
  • M. V. Koulintchenko
    • 1
  • A. Sh. Arziev
    • 1
  • Yu. M. Konstantinov
    • 1
  1. 1.Siberian Institute of Plant Physiology and Biochemistry, Russian Academy of SciencesIrkutskRussia

Personalised recommendations