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Trigger factor assists the refolding of heterodimeric but not monomeric luciferases

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Abstract

The refolding of thermally inactivated protein by ATP-independent trigger factor (TF) and ATP-dependent DnaKJE chaperones was comparatively analyzed. Heterodimeric (αβ) bacterial luciferases of Aliivibrio fischeri, Photobacterium leiognathi, and Vibrio harveyi as well as monomeric luciferases of Vibrio harveyi and Luciola mingrelica (firefly) were used as substrates. In the presence of TF, thermally inactivated heterodimeric bacterial luciferases refold, while monomeric luciferases do not refold. These observations were made both in vivo (Escherichia coli ΔdnaKJ containing plasmids with tig gene) and in vitro (purified TF). Unlike TF, the DnaKJE chaperone system refolds both monomeric and heterodimeric luciferases with equal efficiency.

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Abbreviations

DnaKJE:

chaperone

DnaK:

DnaJ-GrpE

TF:

trigger factor

References

  1. Hartl, F. U., and Hayer-Hartl, M. (2009) Nat. Struct. Mol. Biol., 16, 574–581.

    Article  CAS  PubMed  Google Scholar 

  2. Hoffmann, A., Bukau, B., and Kramer, G. (2010) Biochim. Biophys. Acta, 1803, 650–661.

    Article  CAS  PubMed  Google Scholar 

  3. Merz, F., Boehringer, D., Schaffitzel, C., Pressler, S., Hoffman, A., Maier, T., Rutkowska, A., Lozza, J., Ban, N., Bukau, B., and Deuerling, E. (2008) EMBO J., 27, 1622–1632.

    Article  CAS  PubMed  Google Scholar 

  4. Crooke, E., Guthrie, B., Lecker, S., Lill, R., and Wickner, W. (1988) Cell, 54, 1003–1011.

    Article  CAS  PubMed  Google Scholar 

  5. Lill, R., Crooke, E., Guthrie, B., and Wickner, W. (1988) Cell, 54, 1013–1018.

    Article  CAS  PubMed  Google Scholar 

  6. Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., and Ban, N. (2004) Nature, 431, 590–596.

    Article  CAS  PubMed  Google Scholar 

  7. Baram, D., Pyetan, E., Sittner, A., Auerbach-Nevo, T., Bashan, A., and Yonath, A. (2005) Proc. Natl. Acad. Sci. USA, 102, 12017–12022.

    Article  CAS  PubMed  Google Scholar 

  8. Merz, F., Hoffman, A., Rudkowska, A., Zachmann-Brand, B., and Bukau, B. (2006) J. Biol. Chem., 281, 31963–31971.

    Article  CAS  PubMed  Google Scholar 

  9. Martinez-Hackert, E., and Hendrickson, W. A. (2009) Cell, 138, 923–934.

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  10. Fisher, A. J., Thompson, T. B., Thoden, J. B., Baldwin, T. O., and Rayment, I. (1996) J. Biol. Chem., 271, 21956–21968.

    Article  CAS  PubMed  Google Scholar 

  11. Conti, E., Franks, N. P., and Brick, P. (1996) Structure, 4, 287–298.

    Article  CAS  PubMed  Google Scholar 

  12. Kang, P.-J., and Craig, E. A. (1990) J. Bacteriol., 172, 2055–2064.

    CAS  PubMed Central  PubMed  Google Scholar 

  13. Tchernova, T., and Zavilgelsky, G. B. (1991) Biotekhnologiya, No. 3, 37–40.

    Google Scholar 

  14. Zavilgelsky, G. B., Kotova, V. Y., and Manukhov, I. V. (2003) Mol. Biol. (Moscow), 37, 704–711.

    Article  Google Scholar 

  15. Manukhov, I. V., Duzhii, D. E., and Zavilgelsky, G. B. (1996) Biotekhnologiya, No. 1, 3–8.

    Google Scholar 

  16. Lundovskich, I. A., Leontieva, O. V., Dementieva, E. I., and Ugarova, N. N. (1999) in Proc. 10th Int. Symp. on Bioluminescence and Chemiluminescence: Perspectives for 21st Century (Roda, A., Pazzagli, M., Kricka, L. G., and Stanley, P. E., eds.) John Wiley & Son, Chichester, pp. 420–424.

  17. Boylan, M., Pelletier, J., and Meighen, E. A. (1989) J. Biol. Chem., 264, 1915–1918.

    CAS  PubMed  Google Scholar 

  18. Kolb, V. A., Makeyev, E. V., and Spirin, A. S. (2000) J. Biol. Chem., 275, 16597–16601.

    Article  CAS  PubMed  Google Scholar 

  19. Scholz, C., Stoller, G., Zarnt, T., Fischer, G., and Schmid, F. X. (1997) EMBO J., 16, 54–58.

    Article  CAS  PubMed  Google Scholar 

  20. Estimbekova, E. N., Torgashina, I. G., and Kratasyuk, V. A. (2009) Biochemistry (Moscow), 74, 695–700.

    Article  Google Scholar 

  21. Svetlov, M. S., Kommer, A., Kolb, V. A., and Spirin, A. S. (2006) Protein Sci., 15, 242–247.

    Article  CAS  PubMed  Google Scholar 

  22. Goloubinoff, P., Mogk, A., Ben-Zvi, A., Tomoyasu, T., and Bukau, B. (1999) Proc. Natl. Acad. Sci. USA, 96, 13732–13737.

    Article  CAS  PubMed  Google Scholar 

  23. Liu, C. P., Perrett, S., and Zhou, J. M. (2005) J. Biol. Chem., 280, 13315–13320.

    Article  CAS  PubMed  Google Scholar 

  24. Robin, S., Togashi, D. M., Ryder, A. G., and Wall, J. G. (2009) J. Bacteriol., 191, 1162–1168.

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  25. Rudiger, S., Germeroth, L., Schneider-Mergerier, J., and Bukau, B. (1997) EMBO J., 16, 1501–1507.

    Article  CAS  PubMed  Google Scholar 

  26. Manukhov, I. V., Eroshnikov, G. E., Vyssokikh, M. Y., and Zavilgelsky, G. B. (1999) FEBS Lett., 448, 265–268.

    Article  CAS  PubMed  Google Scholar 

  27. Hesterkamp, T., and Bukau, B. (1998) EMBO J., 17, 4818–4828.

    Article  CAS  PubMed  Google Scholar 

  28. Hoffman, A., Becker, F. H., Zachmann-Brand, B., Deuerling, E., Bukau, B., and Kramer, G. (2012) Mol. Cell, 48, 63–74.

    Article  Google Scholar 

  29. Valkova, M., Szittner, R., and Meighen, E. A. (1999) Biochemistry, 38, 13820–13828.

    Article  CAS  PubMed  Google Scholar 

  30. Tul’kova, N. A., and Sandalova, T. P. (1996) Biochemistry (Moscow), 61, 205–214.

    Google Scholar 

  31. Mashaghi, A., Kramer, G., Betchtlufta, P., Zachmann-Brand, B., Driessen, A. J. M., Bukau, B., and Tans, S. J. (2013) Nature, 500, 98–102.

    Article  CAS  PubMed  Google Scholar 

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Correspondence to G. B. Zavilgelsky.

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Published in Russian in Biokhimiya, 2014, Vol. 79, No. 1, pp. 79–86.

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Melkina, O.E., Goryanin, I.I., Manukhov, I.V. et al. Trigger factor assists the refolding of heterodimeric but not monomeric luciferases. Biochemistry Moscow 79, 62–68 (2014). https://doi.org/10.1134/S000629791401009X

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  • DOI: https://doi.org/10.1134/S000629791401009X

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