Small molecule inhibition of a Group II chaperonin: Pinpointing a loop region within the equatorial domain as necessary for protein refolding

Archives of Biochemistry and Biophysics

Volumn 481, Issue 1, 2009, Pages 45-51

  Bergeron, Lisa M ^a   Shis, David L ^a   Gomez, Lizabeth ^a   Clark, Douglas S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Chaperone; Protein folding; Small molecule inhibition; Structure function relationship; Thermophile

Indexed keywords

6 AMINOPENICILLANIC ACID; 7 AMINOCEPHALOSPORANIC ACID; ADENOSINE TRIPHOSPHATE; CHAPERONIN;

ANISOTROPY; ARTICLE; COMPUTER PROGRAM; CRYSTAL STRUCTURE; FLUORESCENCE; METHANOCALDOCOCCUS JANNASCHII; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; THERMOPHILE; THERMOSTABILITY;

ARCHAEAL PROTEINS; CHAPERONINS; FLUORESCENCE POLARIZATION; METHANOCOCCACEAE; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PENICILLANIC ACID; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING;

ARCHAEA; METHANOCALDOCOCCUS JANNASCHII;

EID: 57449104552     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.10.016     Document Type: Article

References (39)

1. Bergeron L.M., Lee C., and Clark D.S. Biochem. Biophys. Res. Commun. 369 (2008) 707-711
2. Bigotti M.G., and Clarke A.R. Arch. Biochem. Biophys. 474 (2008) 331-339
3. Hartl F.U. Nature 381 (1996) 571-579
4. Weissman J.S., Kashi Y., Fenton W.A., and Horwich A.L. Cell 78 (1994) 693-702
5. Grantcharova V., Alm E.J., Baker D., and Horwich A.L. Curr. Opin. Struct. Biol. 11 (2001) 70-82
6. Hyeon C., Lorimer G.H., and Thirumalai D. Proc. Natl. Acad. Sci. USA 103 (2006) 18939-18944
7. Krishna K.A., Rao G.V., and Rao K.R.S.S. Curr. Protein Pept. Sci. 8 (2007) 418-425
8. Martin J., Mayhew M., Langer T., and Hartl F.U. Nature 366 (1993) 228-233
9. Laksanalamai P., Whitehead T.A., and Robb F.T. Nat. Rev. Microbiol. 2 (2004) 315-324
10. Steinbacher S., and Ditzel L. J. Struct. Biol. 135 (2001) 147-156
11. Horwich A.L., Fenton W.A., Chapman E., and Farr G.W. Annu. Rev. Cell Dev. Biol. 23 (2007) 115-145
12. Klumpp M., Baumeister W., and Essen L.O. Cell 91 (1997) 263-270
13. Saibil H.R., and Ranson N.A. Trends Biochem. Sci. 27 (2002) 627-632
14. Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., and Fersht A.R. Proc. Natl. Acad. Sci. USA 93 (1996) 15024-15029
15. Reissmann S., Parnot C., Booth C.R., Chiu W., and Frydman J. Nat. Struct. Mol. Biol. 14 (2007) 432-440
16. Iizuka R., So S., Inobe T., Yoshida T., Zako T., Kuwajima K., and Yohda M. J. Biol. Chem. 279 (2004) 18834-18839
17. Horovitz A., Bochkareva E.S., and Girshovich A.S. J. Biol. Chem. 268 (1993) 9957-9959
18. Iizuka R., Yoshida T., Maruyama T., Shomura Y., Miki K., and Yohda M. Biochem. Biophys. Res. Commun. 289 (2001) 1118-1124
19. Coluzza I., van der Vies S.M., and Frenkel D. Biophys. J. 90 (2006) 3375-3381
20. Ditzel L., Lowe J., Stock D., Stetter K.O., Huber H., Huber R., and Steinbacher S. Cell 93 (1998) 125-138
21. Yoshida T., Kanzaki T., Iizuka R., Komada T., Zako T., Suzuki R., Maruyama T., and Yohda M. Extremophiles 10 (2006) 451-459
22. Bergeron L.M., Lee C., Tokatlian T., Hollrigl V., and Clark D.S. Biochim. Biophys. Acta 1784 (2008) 368-378
23. L.M. Bergeron, T. Tokatlian, L. Gomez, D.S. Clark, Redirecting the inactivation pathway of penicillin amidase and increasing amoxicillin production via a thermophilic molecular chaperone (2008). doi: 10.1002/bit.22142.
24. Ritchie D.W., and Kemp G.J.L. Proteins 39 (2000) 178-194
25. Basso A., Spizzo P., Toniutti M., Ebert C., Linda P., and Gardossi L. J. Mol. Catal. B Enzym. 39 (2006) 105-111
26. Giordano R.C., Ribeiro M.P.A., and Giordano R.L.C. Biotechnol. Adv. 24 (2006) 27-41
27. Fernandez-Lafuente R., Rosell C.M., and Guisan J.M. Enzyme Microb. Technol. 23 (1998) 305-310
28. Fernandez-Lafuente R., Rosell C.M., Piatkowska B., and Guisan J.M. Enzyme Microb. Technol. 19 (1996) 9-14
29. Jameson D.M., and Sawyer W.H. Methods Enzymol. 246 (1995) 283-300
30. Mendel C.M., and Mendel D.B. Biochem. J. 228 (1985) 269-272
31. Brinkley M. Bioconj. Chem. 3 (1992) 2-13
32. Margolin A.L., Svedas V.K., and Berezin I.V. Biochim. Biophys. Acta 616 (1980) 283-289
33. Gutsche I., Mihalache O., and Baumeister W. J. Mol. Biol. 300 (2000) 187-196
34. Zako T., Iizuka R., Okochi M., Nomura T., Ueno T., Tadakuma H., Yohda M., and Funatsu T. FEBS Lett. 579 (2005) 3718-3724
35. Berezin I.V., Klibanov A.M., Klyosov A.A., Martinek K., and Svedas V.K. FEBS Lett. 49 (1975) 325-328
36. Piotraschke E., Nurk A., Galunsky B., and Kasche V. Biotechnol. Lett. 16 (1994) 119-124
37. Biagi G.L., Barbaro A.M., Gamba M.F., and Guerra M.C. J. Chromatogr. 41 (1969) 371-379
38. Biagi G.L., Barbaro A.M., Guerra M.C., and Gamba M.F. J. Chromatogr. 44 (1969) 195-198
39. Hartl F.U. Nature 371 (1994) 557-559