Catalysis of protein folding by Parvulin

Journal of Molecular Biology

Volumn 273, Issue 3, 1997, Pages 752-762

  Scholz, Christian ^a   Rahfeld, Jens ^b   Fischer, Gunter ^b   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b Forschungsstelle Enzymol P   (Germany)

Author keywords

Autocatalytic folding; Folding enzyme; Parvulin; Prolyl isomerase; Protein folding

Indexed keywords

CYCLOPHILIN; ISOMERASE; PARVULIN; PROLINE; RIBONUCLEASE T1; TETRAPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL BOND; CONTROLLED STUDY; ENTHALPY; ENZYME KINETICS; ESCHERICHIA COLI; ISOMERISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DETERMINATION; PROTEIN FOLDING;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0031592949     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1301     Document Type: Article

References (60)

1. Brandts J. F., Halvorson H. R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due tocistrans. Biochemistry. 14:1975;4953-4963.
2. Callebaut I., Mornon J. P. Trigger factor, one of theEscherichia coli. FEBS Letters. 374:1995;211-215.
3. Eisenstark A., Miller C., Jones J., Leven S. Escherichia coli. Biochem. Biophys. Res. Commun. 188:1992;1054-1059.
4. Evans P. A., Dobson C. M., Kautz R. A., Hatfull G., Fox R. O. Proline isomerism in staphylococcal nuclease characterized by NMR and site directed mutagenesis. Nature. 329:1987;266-268.
5. Fischer G. Peptidyl-prolylcistrans. Agnew. Chem. Int. Ed. 33:1994;1415-1436.
6. Fischer G., Bang H., Mech C. Nachweis einer enzymkatalyse für diecistrans. Biomed. Biochim. Acta. 43:1984;1101-1111.
7. Franke E. K., Yuan H. E. H., Luban J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature. 372:1994;359-362.
8. Galat A., Metcalfe S. M. Peptidylprolinecistrans. Prog. Biophys. Mol. Biol. 63:1995;67-118.
9. Gamble T. R., Vajdos F. F., Yoo S. H., Worthylake D. K., Houseweart M., Sundquist W. I., Hill C. P. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell. 87:1996;1285-1294.
10. Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
11. Haandrikman A. J., Kok J., Laan H., Soemitro S., Ledeboer A. M., Konings W. N., Venema G. Identification of a gene required for maturation of an extracellular lactococcal serine proteinase. J. Bacteriol. 171:1989;2789-2794.
12. Hani J., Stumpf G., Domdey H. PTF1 encodes an essential protein inSaccharomyces cerevisiae. FEBS Letters. 365:1995;198-202.
13. Harrison R. K., Stein R. L. Mechanistic studies of enzymic and nonenzymic prolylcistrans. J. Am. Chem. Soc. 114:1992;3464-3471.
14. Hesterkamp T., Hauser S., Lütcke H., Bukau B. Escherichia coli. Proc. Natl Acad. Sci. USA. 93:1996;4437-4441.
15. Jacobs M., Anderson J. B., Kontinen V., Sarvas M. Bacillus subtilisin vivo. Mol. Microbiol. 8:1993;957-966.
16. Kiefhaber T., Grunert H.-P., Hahn U., Schmid F. X. Replacement of acis. Biochemistry. 29:1990;6475-6480.
17. Kim P. S., Baldwin R. L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:1982;459-489.
18. Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
19. Kofron J. L., Kuzmic P., Kishore V., Colonbonilla E., Rich D. H. Determination of kinetic constants for peptidyl prolylcistrans. Biochemistry. 30:1991;6127-6134.
20. Kontinen V. P., Sarvas M. The PrsA lipoprotein is essential for protein secretion inBacillus subtilis. Mol. Microbiol. 8:1993;727-737.
21. Kördel J., Forsen S., Drakenberg T., Chazin W. J. The rate and structural consequences of prolinecistranscis. Biochemistry. 29:1990;4400-4409.
22. Lang K., Schmid F. X., Fischer G. Catalysis of protein folding by prolyl isomerase. Nature. 329:1987;268-270.
23. Lazar S. W., Kolter R. SurA assists the folding ofEscherichia coli. J. Bacteriol. 178:1996;1770-1773.
24. Lin L.-N., Hasumi H., Brandts J. F. Catalysis of proline isomerization during protein folding reactions. Biochim. Biophys. Acta. 956:1988;256-266.
25. Lu K. P., Hanes S. D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547.
26. Macarthur M. W., Thornton J. M. Influence of proline residues on protein conformation. J. Mol. Biol. 218:1991;397-412.
27. Matouschek A., Rospert S., Schmid K., Glick B. S., Schatz G. Cyclophilin catalyzes protein folding in yeast mitochondria. Proc. Natl Acad. Sci. USA. 92:1995;6319-6323.
28. Mayr L. M., Odefey C., Schutkowski M., Schmid F. X. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry. 35:1996;5550-5561.
29. Missiakas D., Raina S. Protein misfolding in the cell envelope ofEscherichia coli. Trends Biochem. Sci. 22:1997;59-63.
30. Missiakas D., Betton J. M., Raina S. New components of protein folding in extracytoplasmic compartments ofEscherichia coli. Mol. Microbiol. 21:1996;871-884.
31. Mücke M., Schmid F. X. Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry. 33:1994;14608-14619.
32. Neurath H. Limited proteolysis, domains, and the evolution of protein structure. Chem. Script. sect. B. 27:1986a;221-229.
33. Neurath H. The versatility of proteolytic enzymes. J. Cell. Biochem. 32:1986b;35-49.
34. Nissen Meyer J., Lillehaug D., Nes I. F. The plasmid-encoded lactococcal envelope-associated proteinase is encoded by a chromosomal gene inLactococcus lactis. Appl. Environ. Microbiol. 58:1992;750-753.
35. Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
36. Rahfeld J. U., Rücknagel K. P., Schelbert B., Ludwig B., Hacker J., Mann K., Fischer G. Confirmation of the existence of a third family among peptidyl-prolylcistrans. FEBS Letters. 352:1994a;180-184.
37. Rahfeld J.-U., Schierhorn A., Mann K.-H., Fischer G. A novel peptidyl-prolylcistransEscherichia coli. FEBS Letters. 343:1994b;65-69.
38. Ranganathan R., Lu K. P., Hunter T., Noel J. P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell. 89:1997;875-886.
39. Rassow J., Mohrs K., Koidl S., Barthelmess I. B., Pfanner N., Tropschug M. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15:1995;2654-2662.
40. Rouviere P. E., Gross C. A. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:1996;3170-3182.
41. Santoro M. M., Bolen D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
42. Schittkowski K. NLSFIT; a FORTRAN code for parameter estimation in differential equations and explicit model functions. 1993;Universität Bayreuth.
43. Schmid F. X. Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol. 131:1986;71-82.
44. Schmid F. X. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22:1993;123-143.
45. Schmid F. X., Baldwin R. L. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc. Natl Acad. Sci. USA. 75:1978;4764-4768.
46. Schmid F. X., Mayr L. M., Mücke M., Schönbrunner E. R. Prolyl isomerases: role in protein folding. Advan. Protein Chem. 44:1993;25-66.
47. Scholz C., Zarnt T., Kern G., Lang K., Burtscher H., Fischer G., Schmid F. X. Autocatalytic folding of the folding catalyst FKBP12. J. Biol. Chem. 271:1996;12703-12707.
48. Scholz C., Stoller G., Zarnt T., Fischer G., Schmid F. X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16:1997;54-58.
49. Schönbrunner E. R., Mayer S., Tropschug M., Fischer G., Takahashi N., Schmid F. X. Catalysis of protein folding by cyclophilins from different species. J. Biol. Chem. 266:1991;3630-3635.
50. Schreiber S. L. Chemistry and biology of the immunophilins and their immunosuppresive ligands. Science. 251:1991;283-287.
51. Stein R. L. Mechanism of enzymatic and nonenzymatic prolylcistrans. Advan. Protein Chem. 44:1993;1-24.
52. Stewart D. E., Sarkar A., Wampler J. E. Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214:1990;253-260.
53. Stoller G., Rücknagel K. P., Nierhaus K., Schmid F. X., Fischer G., Rahfeld J.-U. Identification of the peptidyl-prolylcistransEscherichia coli. EMBO J. 14:1995;4939-4948.
54. Takahashi K., Uchida T., Egami F. Ribonuclease T1: structure and function. Advan. Biophys. 1:1970;53-98.
55. Thali M., Bukovsky A., Kondo E., Rosenwirth B., Walsh C. T., Sodroski J., Göttlinger H. G. Functional association of cyclophilin A with HIV-1 virions. Nature. 372:1994;363-365.
56. Valent Q. A., Kendall D. A., High S., Kusters R., Oudega B., Luirink J. Early events in preprotein recognition inE coli. EMBO J. 14:1995;5494-5505.
57. Veeraraghavan S., Holzman T. F., Nall B. T. Autocatalyzed protein folding. Biochemistry. 35:1996;10601-10607.
58. Wang T. W., Li B. Y., Danielson P. D., Shah P. C., Rockwell S., Lechleider R. J., Martin J., Manganaro T., Donahoe P. K. The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors. Cell. 86:1996;435-444.
59. Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F. X., Fischer G. Modular structure of the trigger factor required for high activity in protein folding. J. Mol. Biol. 1997.
60. Zhao Y. D., Chen Y. Q., Schutkowski M., Fischer G., Ke H. M. Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity. Structure. 5:1997;139-146.