Thermal unfolding of Escherichia coli trigger factor studied by ultra-sensitive differential scanning calorimetry

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 11, 2008, Pages 1728-1734

  Fan, Dong Jie ^a,c   Ding, Yan Wei ^b   Pan, Xian Ming ^a   Zhou, Jun Mei ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Cross linking; DSC; Intermediate; Protein folding; Thermal denaturation; Trigger factor

Indexed keywords

CHAPERONE; DIMER; MONOMER; MUTANT PROTEIN; POLYPEPTIDE; TRIGGER FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; CARBOXY TERMINAL SEQUENCE; CELL DAMAGE; CELL STRESS; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; THERMOSTABILITY;

CALORIMETRY, DIFFERENTIAL SCANNING; CROSS-LINKING REAGENTS; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK RESPONSE; MODELS, CHEMICAL; MUTANT PROTEINS; PEPTIDYLPROLYL ISOMERASE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SENSITIVITY AND SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 54049120607     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.002     Document Type: Article

References (31)

1. Hesterkamp T., Hauser S., Lütcke H., and Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 4437-4441
2. Valent Q.A., Kendall D.A., High S., Oudega B., and Luirink J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14 (1995) 5494-5505
3. Stoller G., Rücknagel K.P., Nierhaus K.H., Schmid F.X., Fischer G., and Rahfeld J.U. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14 (1995) 4939-4948
4. Scholz C., Stoller G., Fischer G., and Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16 (1997) 54-58
5. Kramer G., Rauch T., Rist W., Vorderwülbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., and Bukau B. L23 protein functions as a chaperone docking site on the ribosome. Nature 419 (2002) 171-174
6. Blaha G., Wilson D.N., Stoller G., Fischer G., Willumeit R., and Nierhaus K.H. Localization of the trigger factor binding site on the ribosomal 50S subunit. J. Mol. Biol. 326 (2003) 887-897
7. Stoller G., Tradler T., Rücknagel K.P., Rahfeld J.U., and Fischer G. An 11.8 kDa proteolytic fragment of E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity. FEBS Lett. 384 (1996) 117-122
8. Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F.X., and Fischer G. Modular structure of the trigger factor required for high activity in protein folding. J. Mol. Biol. 271 (1997) 827-837
9. Hesterkamp T., Deuerling E., and Bukau B. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J. Biol. Chem. 272 (1997) 21865-21871
10. Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., and Yonath A. Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 12017-12022
11. Hoffmann A., Merz F., Rutkowska A., Zachmann-Brand B., Deuerling E., and Bukau B. Trigger factor forms a protective shield for nascent polypeptides at the ribosome. J. Biol. Chem. 281 (2006) 6539-6545
12. Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U., and Georgopoulos C. In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 5 (2004) 195-200
13. Kramer G., Rutkowska A., Wegrzyn R., Patzelt H., Kurz T.A., Merz F., Rauch T., Vorderwülbecke S., Deuerling E., and Bukau B. Functional dissection of Escherichia coli trigger factor: unravelling the function of individual domains. J. Bacteriol. 186 (2004) 3777-3784
14. Merz F., Hoffmann A., Rutkowska A., Zachmann-Brand B., Bukau B., and Deuerling E. The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J. Biol. Chem. 281 (2006) 31963-31971
15. Ferbitz L., Patzelt H., Bukau B., Deuerling E., and Ban N. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431 (2004) 590-596
16. Baldwin R.L., and Rose G.D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24 (1999) 77-83
17. Arai M., and Kuwajima K. Role of the molten globule state in protein folding. Adv. Protein Chem. 53 (2000) 209-282
18. Fink A.L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24 (1995) 495-522
19. Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
20. Liu C.P., Li Z.Y., Huang G.C., Perrett S., and Zhou J.M. Two distinct intermediates of trigger factor are populated during guanidine denaturation. Biochimie 87 (2005) 1023-1031
21. Liu C.P., Perrett S., and Zhou J.M. Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding. J. Biol. Chem. 280 (2005) 13315-13320
22. Freire E., and Biltonen R.L. Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems. Biopolymers 17 (1978) 463-479
23. Shi Y., Fan D.J., Li S.X., Zhang H.J., Perrett S., and Zhou J.M. Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor. Protein Sci. 16 (2007) 1165-1175
24. Zeng L.L., Yu L., Li Z.Y., Perrett S., and Zhou J.M. Effect of C-terminal truncation on the molecular chaperone function and dimerization of Escherichia coli trigger factor. Biochimie 88 (2006) 613-619
25. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
26. Ludlam A.V., Moore B.A., and Xu Z.H. The crystal structure of ribosomal chaperon trigger factor from vibrio cholerae. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 13436-13441
27. Kaiser C.M., Chang H.C., Agashe V.R., Lakshmipathy S.K., Etchells S.A., Hartl M., Hayer-Hartl F.U., and Barral J.M. Real-time observation of trigger factor function on translating ribosomes. Nature 444 (2006) 455-460
28. Maier R., Eckert B., Scholz C., Lilie H., and Schmid F.X. Interaction of trigger factor with the ribosome. J. Mol. Biol. 326 (2003) 585-592
29. Patzelt H., Kramer G., Rauch T., Schönfeld H.J., Bukau B., and Deuerling E. Three-state equilibrium of Escherichia coli trigger factor. Biol. Chem. 383 (2002) 1611-1619
30. Liu C.P., and Zhou J.M. Trigger factor-assisted folding of bovine carbonic anhydrase II. Biochem. Biophys. Res. Commun. 313 (2004) 509-515
31. Patzelt H., Rüdiger S., Brehmer D., Kramer G., Vorderwülbecke S., Schaffitzel E., Waitz A., Hesterkamp T., Dong L., Schneider-Mergener J., Bukau B., and Deuerling E. Binding specificity of Escherichia coli trigger factor. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 14244-14249