Primary Structure of a Human Mitochondrial Protein Homologous to the Bacterial and Plant Chaperonins and to the 65-Kilodalton Mycobacterial Antigen

LITERATURE CITED

• Ellis, R. J.. 1987. Proteins a molecular chaperones. Nature (London) 328:378–379.
   PubMed Web of Science ®Google Scholar
• Garnier, J., D. J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods of predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97–120.
   PubMed Web of Science ®Google Scholar
• Goloubinoff, P., A. A. Gatenby, and G. H. Lorimer. 1989. GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature (London) 337:44–47.
   PubMedGoogle Scholar
• Gupta, R. S., and R. A. Austin. 1987. Mitochondrial matrix localization of a protein affected in mutants resistant to the microtubule inhibitor podophyllotoxin. Eur. J. Cell Biol. 45:170–176.
   PubMedGoogle Scholar
• Gupta, R. S., and A. K. Dudani. 1987. Mitochondrial binding of a protein affected in mutants resistant to the microtubule inhibitor podophyllotoxin. Eur. J. Cell Biol. 44:278–285.
   PubMedGoogle Scholar
• Gupta, R. S., and T. K. W. Ho, M. R. K. Moffat, and R. Gupta. 1982. Podophyllotoxin-resistant mutants of Chinese hamster ovary cells: alteration in a microtubule associated protein. J. Biol. Chem. 257:1071–1078.
   PubMed Web of Science ®Google Scholar
• Gupta, R. S., T. J. Venner, and A. Chopra. 1985. Genetic and biochemical studies with mutants of mammalian cells affected in microtubule related proteins other than tubulin: mitochondrial localization of a microtubule related protein. Can. J. Biochem. Cell Biol. 63:489–502.
   PubMedGoogle Scholar
• Hemmingsen, S. M., C. Woolford, S. M. van der Vies, K. Tilly, D. T. Dennis, C. P. Georgopoulos, R. W. Hendrix, and R. J. Ellis. 1988. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature (London) 33:330–334.
   Google Scholar
• Hoffman, W., J. K. Franz, and W. W. Franke. 1985. Amino acid sequence microheterogeneities of basic (type II) cytokeratins of Xenopus laevis epidermis and evolutionary conservativity of helical and nonhelical domains. J. Mol. Biol. 184:713–724.
   PubMedGoogle Scholar
• Holoshitz, J., A. Klajman, I. Drucker, J. Lapidot, A. Yaretzky, A. Frankel, W. Van Eden, and I. R. Cohen. 1986. T lymphocytes of rheumatoid arthritis patients show augmented reactivity to a fraction of mycobacteria cross-reactive with cartilage. Lancet 11:305–309.
   Google Scholar
• Huynh, T.-V., R. A. Young, and R. W. Davis. 1985. Construction and screening cDNA libraries in λgt10 and λgt11, p. 49–78. D. M. Glover (ed.), DNA cloning, vol. 1. IRL Press, Oxford.
   Google Scholar
• Kozak, M.. 1987. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:8125–8149.
   PubMed Web of Science ®Google Scholar
• McMullin, T. W., and R. L. Hallberg. 1987. A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophilia. Mol. Cell. Biol. 7:4414–4423.
   PubMedGoogle Scholar
• McMullin, T. W., and R. L. Hallberg. 1988. A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol. Cell. Biol. 8:371–380.
   PubMedGoogle Scholar
• Mehra, V., D. Sweetser, and R. A. Young. 1986. Efficient mapping of protein antigenic determinants. Proc. Natl. Acad. Sci. USA 83:7013–7017.
   PubMed Web of Science ®Google Scholar
• Schatz, G.. 1987. Signals guiding proteins to their correct locations in mitochondria. Eur. J. Biochem. 165:1–6.
   PubMedGoogle Scholar
• Schwartz, R. M., and M. O. Dayhoff. 1978. Origins of prokaryotes, eukaryotes, mitochondria and chloroplasts. A perspective is derived from protein and nucleic acid sequence data. Science 199:395–403.
   PubMed Web of Science ®Google Scholar
• Shinnick, T. M.. 1987. The 65-kilodalton antigen of Mycobacterium tuberculosis. J. Bacteriol. 169:1080–1088.
   PubMedGoogle Scholar
• Shinnick, T. M., D. Sweetser, J. Thole, J. van Embden, and R. A. Young. 1987. The etiologic agents of leprosy and tuberculosis share an immunoreactive protein antigen with the vaccine strain Mycobacterium bovis BCG. Infect. Immun. 55:1932–1935.
   PubMedGoogle Scholar
• Thole, J. E. R., W. J. Kealen, A. H. J. Kolk, D. G. Groothuis, L. G. Berwald, R. H. Tiesjema, and J. D. A. van Embden. Characterization, sequence determination and immunogenicity of a 64-kilodalton protein of Mycobacterium bovis BCG expressed in Escherichia coli K-12. Infect. Immun. 55:1466–1475.
   PubMedGoogle Scholar
• van Eden, W., J. E. R. Thole, R. van der Zee, A. Noordzij, J. D. A. van Embden, E. J. Hensen, and I. R. Cohen. 1988. Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis. Nature (London) 331:171–173.
   PubMed Web of Science ®Google Scholar
• Waldinger, D., C. Eckerskorn, F. Lottspeich, and H. Cleve. 1988. Amino acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (rubisco binding protein). Biol. Chem. Hoppe-Seyler 369:1185–1189.
   PubMedGoogle Scholar
• Young, D., R. Lathigra, R. Hendrix, D. Sweetser, and R. A. Young. 1988. Stress proteins are immune targets in leprosy and tuberculosis. Proc. Natl. Acad. Sci. USA 85:4267–4270.
   PubMed Web of Science ®Google Scholar