메뉴 건너뛰기




Volumn 369, Issue 2, 2008, Pages 707-711

Identification of a critical chaperoning region on an archaeal recombinant thermosome

Author keywords

Chaperonin; Organic solvent; Protein folding; Structure function relationship; Thermophile

Indexed keywords

ADENOSINE 5' PHOSPHOSULFATE; CHAPERONE; CHAPERONIN; CITRATE SYNTHASE; RECOMBINANT PROTEIN; SOLVENT; THERMOSOME; UNCLASSIFIED DRUG;

EID: 40849102389     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.02.103     Document Type: Article
Times cited : (5)

References (21)
  • 3
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin J., Mayhew M., Langer T., and Hartl F.U. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366 (1993) 228-233
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 5
    • 0035783334 scopus 로고    scopus 로고
    • Review: nucleotide binding to the thermoplasma thermosome: implications for the functional cycle of group II chaperonins
    • Steinbacher S., and Ditzel L. Review: nucleotide binding to the thermoplasma thermosome: implications for the functional cycle of group II chaperonins. J. Struct. Biol. 135 (2001) 147-156
    • (2001) J. Struct. Biol. , vol.135 , pp. 147-156
    • Steinbacher, S.1    Ditzel, L.2
  • 6
    • 2142806742 scopus 로고    scopus 로고
    • Minimal protein-folding systems in hyperthermophilic archaea
    • Laksanalamai P., Whitehead T.A., and Robb F.T. Minimal protein-folding systems in hyperthermophilic archaea. Nat. Rev. Microbiol. 2 (2004) 315-324
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 315-324
    • Laksanalamai, P.1    Whitehead, T.A.2    Robb, F.T.3
  • 8
    • 33749822818 scopus 로고    scopus 로고
    • Contribution of the C-terminal region to the thermostability of the archaeal group II chaperonin from Thermococcus sp. strain KS-1
    • Yoshida T., Kanzaki T., Iizuka R., Komada T., Zako T., Suzuki R., Maruyama T., and Yohda M. Contribution of the C-terminal region to the thermostability of the archaeal group II chaperonin from Thermococcus sp. strain KS-1. Extremophiles 10 (2006) 451-459
    • (2006) Extremophiles , vol.10 , pp. 451-459
    • Yoshida, T.1    Kanzaki, T.2    Iizuka, R.3    Komada, T.4    Zako, T.5    Suzuki, R.6    Maruyama, T.7    Yohda, M.8
  • 9
    • 2442592916 scopus 로고    scopus 로고
    • Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin
    • Iizuka R., So S., Inobe T., Yoshida T., Zako T., Kuwajima K., and Yohda M. Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin. J. Biol. Chem. 279 (2004) 18834-18839
    • (2004) J. Biol. Chem. , vol.279 , pp. 18834-18839
    • Iizuka, R.1    So, S.2    Inobe, T.3    Yoshida, T.4    Zako, T.5    Kuwajima, K.6    Yohda, M.7
  • 10
    • 34247635168 scopus 로고    scopus 로고
    • Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins
    • Reissmann S., Parnot C., Booth C.R., Chiu W., and Frydman J. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat. Struct. Mol. Biol. 14 (2007) 432-440
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 432-440
    • Reissmann, S.1    Parnot, C.2    Booth, C.R.3    Chiu, W.4    Frydman, J.5
  • 11
    • 0035930935 scopus 로고    scopus 로고
    • Glycine at the 65th position plays an essential role in ATP-dependent protein folding by archael group II chaperonin
    • Iizuka R., Yoshida T., Maruyama T., Shomura Y., Miki K., and Yohda M. Glycine at the 65th position plays an essential role in ATP-dependent protein folding by archael group II chaperonin. Biochem. Biophys. Res. Commun. 289 (2001) 1118-1124
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 1118-1124
    • Iizuka, R.1    Yoshida, T.2    Maruyama, T.3    Shomura, Y.4    Miki, K.5    Yohda, M.6
  • 12
    • 0027314946 scopus 로고
    • The N-terminus of the molecular chaperonin groel is a crucial structural element for its assembly
    • Horovitz A., Bochkareva E.S., and Girshovich A.S. The N-terminus of the molecular chaperonin groel is a crucial structural element for its assembly. J. Biol. Chem. 268 (1993) 9957-9959
    • (1993) J. Biol. Chem. , vol.268 , pp. 9957-9959
    • Horovitz, A.1    Bochkareva, E.S.2    Girshovich, A.S.3
  • 13
    • 38549175156 scopus 로고    scopus 로고
    • Chaperone function in organic co-solvents: experimental characterization and modeling of a hyperthermophilic chaperone subunit from Methanocaldococcus jannaschii
    • Bergeron L.M., Lee C., Tokatlian T., Hollrigl V., and Clark D.S. Chaperone function in organic co-solvents: experimental characterization and modeling of a hyperthermophilic chaperone subunit from Methanocaldococcus jannaschii. Biochim. Biophys. Acta 1784 (2008) 368-378
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 368-378
    • Bergeron, L.M.1    Lee, C.2    Tokatlian, T.3    Hollrigl, V.4    Clark, D.S.5
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng M.A.L.J.K., and Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectr. 5 (1994) 976-989
    • (1994) J. Am. Soc. Mass Spectr. , vol.5 , pp. 976-989
    • Eng, M.A.L.J.K.1    Yates, J.R.2
  • 15
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: influence of denaturant and folding assistants
    • Zhi W., Landry S.J., Gierasch L.M., and Srere P.A. Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci. 1 (1992) 522-529
    • (1992) Protein Sci. , vol.1 , pp. 522-529
    • Zhi, W.1    Landry, S.J.2    Gierasch, L.M.3    Srere, P.A.4
  • 16
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner J., Grallert H., and Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290 (1998) 323-338
    • (1998) Methods Enzymol. , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 18
    • 18744389426 scopus 로고    scopus 로고
    • ATP-induced structural change of the thermosome is temperature-dependent
    • Gutsche I., Holzinger J., Rauh N., Baumeister W., and May R.P. ATP-induced structural change of the thermosome is temperature-dependent. J. Struct. Biol. 135 (2001) 139-146
    • (2001) J. Struct. Biol. , vol.135 , pp. 139-146
    • Gutsche, I.1    Holzinger, J.2    Rauh, N.3    Baumeister, W.4    May, R.P.5
  • 19
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., and Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 (1997) 741-750
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 20
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
    • Todd M.J., Viitanen P.V., and Lorimer G.H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265 (1994) 659-666
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 21
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel L., Lowe J., Stock D., Stetter K.O., Huber H., Huber R., and Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93 (1998) 125-138
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.