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Faculty of Health Sciences

Gupta Lab

Mitochondrial Proteins

This area of research is no longer being pursued in our lab. For our work in this area, please refer to our publications.

Studies on mitochondrial and heat shock proteins

Mitochondria are essential cellular organelles responsible for production of most of the cellular energy. It is currently believed that under normal conditions, proteins made within the mitochondria or targeted to this organelle reside and function only within this compartment.

However, in recent years, numerous examples of mit-proteins, both nuclear DNA encoded and mit-DNA encoded, that are present at specific extramitochondrial sites have been discovered. Many of these proteins carry out novel functions at these extra-mitochondrial locations.

My lab has pioneered the study of these proteins and our work strongly suggests that proteins can exit from mitochondria to other specific cellular locations and their functions are not limited to within mitochondria.

  1. Bowes, T. and Gupta, R. S. (2008) Novel mitochondrial extensions provide evidence for a link between microtubule-directed movement and mitochondrial fission. Biochem Biophys Res Commun. 376(1): 40-5.
  2. Gupta, R. S., Ramachandra, N. B., Bowes, T. and Singh, B. (2008) Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10. Novartis Found Symp. 291: 59-68.
  3. Bowes, T., Singh, B. and Gupta, R. S. (2006) Subcellular localization of Fumarase in mammalian cells and tissues. Histochem. Cell Biology. Nov 17 (Epub).
  6. Bowes, T.J. and Gupta, R.S. (2005) Induction of mitochondrial fusion by cysteine-alkylators ethacrynic acid and N-ethylmaleimide. J. Cell. Physiol. 202: 796-804.
  7. Gupta, R.S., Bowes, T., Sadacharan, S. and Singh, B. (2005) Intracellular disposition of Mitochondrial Molecular Chaperones (Hsp60, mHsp70, Cpn10 and TRAP-1). In “Extracellular Biology of Molecular Chaperones” B. Henderson and A.G. Pockley (Eds.), Cambridge University Press (in press).
  8. Cechetto, J.D., Sadacharan, S.K., Berk, P.D. and Gupta, R. S. (2002) Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues. Histol. Histopathol. 17, 353-364.
  9. Bowes, T.J. and Gupta, R.S. (2004) Induction of mitochondrial fusion by cysteine-alkylators ethacrynic acid and N-ethylmaleimide. J. Cell. Physiol. 202:796-804.
  11. Soltys, B.J., D.W. Andrews, Jemmerson,R. and Gupta, R.S. (2001) Cytochrome-C localizes in secretory granules in pancreas and anterior pituitary. Cell Biol. Internat. 25: 331-338.
  14. Soltys, B.J., Kang, D. and Gupta, R.S. (2000) Localization of P32 protein (gC1q-R) in mitochondria and at specific extramitochondrial locations in normal tissues. Histochem. Cell Biol. 114:245-255.
  16. Soltys , B. J. and Gupta, R.S. (1999) Mitochondrial-matrix proteins at unexpected locations: are they exported? Trends Biochem. Sci. 24: 174-177.
  17. Khan, I.U., Wallin, R., Gupta, R.S. and Kammer, G. L. (1998) Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane. Proc. Natl. Acad. Sci. USA. 95: 10425-10430.
  18. Singh, B., Soltys, B., Wu, Z-C., Patel, H.V., Freeman, K.B. and Gupta, R.S. (1997) Cloning and some novel characteristics of mitochondrial HSP70 from Chinese hamster cells. Exp. Cell Res. 234: 205-216.
  20. Soltys, B.J. and Gupta, R.S. (1996) Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biology International 21: 315-320.
  21. Xu, Q., Schett, G., Seitz, C.S., Hu, Y., Gupta, R.S. and Wick, G. (1994) Surface staining and cytotoxic activity of heat-shock protein 60 antibody in stressed aortic endothelial cells. Circulation Res. 75: 1078-1085.
  24. Kaur, I., Voss, S.D., Gupta, R.S., Schell, K., Fisch, P. and Sondel, P.M. (1993) Human peripheral gamma delta T cells recognize hsp60 molecules on Daudi Burkitt’s lymphoma cells. J. Immunol. 150: 2046-2055.
  27. Viitanen, P.V., Lorimer, G.H., Seetharam, R., Gupta, R.S., Oppenheim, J., Thomas, J.O. and Cowan, N.J. (1992) Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. J. Biol. Chem. 267: 695-698.
  28. Venner, T.J. and Gupta, R.S. (1990) Nucleotide sequence of mouse HSP60 (chaperonin, GroEL homolog) cDNA. Biochim. Biophys. Acta 1087: 336-338.
  31. Gupta, R.S. (1990) Mitochondria, molecular chaperone proteins and the in vivo assembly of microtubules. Trends in Biochem. Sc. 15: 415-418.
  32. Singh, B., Patel, H.V., Ridley, R.G., Freeman, K.B. and Gupta, R.S. (1990). Mitochondrial import of the human chaperonin (HSP60) protein. Biochem. Biophys. Res. Commun. 169: 391-396.
  34. Picketts, D.J., Mayanil, C.S.K. and Gupta, R.S. (1989). Molecular cloning of a Chinese hamster mitochondrial protein related to the “chaperonin” family of bacterial and plant proteins. J. Biol. Chem. 264: 12001-12008.
  36. Jindal, S., Dudani, A.K., Singh, B., Harley, C.B. and Gupta, R.S (1989). Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Mol. Cell Biol. 9: 2279-2283. [Abstract]
  40. Gupta, R.S., Ho, T.K.W., Moffat, M.R.K. and Gupta, R. (1982). Podophyllotoxin-resistant mutants of Chinese hamster ovary cells. Alteration in a microtubule-associated protein. J. Biol. Chem. 257: 1071-1078.