Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family

Protein Science

Volumn 15, Issue 2, 2006, Pages 242-247

  Svetlov, Maxim S ^a   Kommer, Aigar ^a   Kolb, Vyacheslav A ^a   Spirin, Alexander S ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Cotranslational folding; Hsp70 chaperones; Specific activity; Trigger factor

Indexed keywords

CHAPERONE; FIREFLY LUCIFERASE; HEAT SHOCK PROTEIN 70;

ARTICLE; CELL FREE SYSTEM; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SYNTHESIS; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FAMILY; PROTEIN FOLDING;

CELL-FREE SYSTEM; ESCHERICHIA COLI; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES, FIREFLY; MOLECULAR CHAPERONES; PROTEIN BIOSYNTHESIS; PROTEIN FOLDING; PROTEIN MODIFICATION, TRANSLATIONAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 31344479583     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051752506     Document Type: Article

References (24)

1. Agashe, V.R., Guha, S., Chang, H.-C., Genevaux, P., Hayer-Hartl, M., Stemp, M., Georgopoulos, C., Hartl, F.U., and Barral, J.M. 2004. Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed. Cell 117: 199-209.
2. Buchberger, A., Schröder, H., Hesterkamp, T., Schönfeld, H.-J., and Bukau, B. 1996. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261: 328-333.
3. Chekulaeva, M.N., Kurnasov, O.V., Shirokov, V.A., and Spirin, A.S. 2001. Continuous-exchange cell-free protein-synthesizing system: Synthesis of HIV-1 antigen Nef. Biochem. Biophys. Res. Commun. 280: 914-917.
4. Conti, E., Francs, N.P., and Brick, P. 1996. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4: 287-298.
5. Frydman, J. 2001. Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu. Rev. Biochem. 70: 603-647.
6. Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F.U. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370: 111-117.
7. Gilmore, R., Coffey, M.C., Leone, G., McLure, K., and Lee, P.W.K. 1996. Cotranslational trimerization of the reovirus cell attachment protein. EMBO J. 15: 2651-2658.
8. Hendrick, J.P., Langer, T., Davis, T.A., Hartl, F.U., and Wiedmann, M. 1993. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. 90: 10216-10220.
9. Herbst, R., Schafer, U., and Seckler, R. 1997. Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase. J. Biol. Chem. 272: 7099-7105.
10. Hesterkamp, T. and Bukau, B. 1998. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17: 4818-4828.
11. Kolb, V.A., Makeyev, E.V., and Spirin, A.S. 1994. Folding of firefly luciferase during translation in a cell-free system. EMBO J. 13: 3631-3637.
12. _. 2000. Co-translational folding of an eukaryotic multidomain protein in a prokaryotic translation system. J. Biol. Chem. 275: 16597-16601.
13. Komar, A.A., Kommer, A., Krasheninnikov, I.A., and Spirin, A.S. 1997. Cotranslational folding of globin. J. Biol. Chem. 272: 10646-10651.
14. Nicola, A.V., Chen, W., and Helenius, A. 1999. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells. Nat. Cell Biol. 1: 341-345.
15. Schägger, H. and von Jagow, G. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368-379.
16. Scholz, C., Stoller, G., Zarnt, T., Fischer, G., and Schmid, F.X. 1997. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16: 54-58.
17. Schröder, H., Langer, T., Hartl, F.-U., and Bukau, B. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12: 4137-4144.
18. Shimizu, Y., Inoue, A., Tomary, Y., Suzuki, T., Yokogawa, T., Nishikawa, K., and Ueda, T. 2001. Cell-free translation reconstituted with purified components. Nat. Biotechnol. 19: 751-755.
19. Stoller, G., Rücknagel, K.P., Nierhaus, K.H., Schmid, F.X., Fischer, G., and Rahfeld, J.-U. 1995. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14: 4939-4948.
20. Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F.U. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. 91: 10345-10349.
21. Teter, S.A., Houry, W.A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., and Hartl, F.U. 1999. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97: 755-765.
22. Tyedmers, J., Brunke, M., Lechte, M., Sandholzer, U., Dierks, T., Schlotterhose, P., Schmidt, B., and Zimmermann, R. 1996. Efficient folding of firefly luciferase after transport into mammalian microsomes in the absence of luminal chaperones and folding catalysts. J. Biol. Chem. 271: 19509-19513.
23. Zako, T., Deguchi, H., Kitayama, A., Ueda, H., and Nagamune, T. 2000. Refolding of firefly luciferase immobilized on agarose beads. J. Biochem. 127: 351-354.
24. Zubay, G. 1973. In vitro synthesis of protein in microbial systems. Annu. Rev. Genet. 7: 267-287.