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Volumn 16, Issue 4, 2007, Pages 626-634

A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii

Author keywords

Heat shock response; Molecular chaperones; Prefoldin; Protein filaments

Indexed keywords

CHAPERONE; PROTEIN PREFOLDIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33947720464     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062599907     Document Type: Article
Times cited : (37)

References (31)
  • 1
    • 18944394260 scopus 로고    scopus 로고
    • Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock
    • Boonyaratanakornkit, B.B., Simpson, A.J., Whitehead, T.A., Fraser, C.M., El-Sayed, N.M., and Clark, D.S. 2005. Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock. Environ. Microbiol. 7: 789-797.
    • (2005) Environ. Microbiol , vol.7 , pp. 789-797
    • Boonyaratanakornkit, B.B.1    Simpson, A.J.2    Whitehead, T.A.3    Fraser, C.M.4    El-Sayed, N.M.5    Clark, D.S.6
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner, J., Grallert, H., and Jakob, U. 1998. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290: 323-338.
    • (1998) Methods Enzymol , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 4
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis, R.J. 2001. Macromolecular crowding: An important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11: 114-119.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 5
    • 0034687748 scopus 로고    scopus 로고
    • Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry
    • Fandrich, M., Tito, M.A., Leroux, M.R., Rostom, A.A., Hartl, F.U., Dobson, C.M., and Robinson, C.V. 2000. Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry. Proc. Natl. Acad. Sci. 97: 14151-14155.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 14151-14155
    • Fandrich, M.1    Tito, M.A.2    Leroux, M.R.3    Rostom, A.A.4    Hartl, F.U.5    Dobson, C.M.6    Robinson, C.V.7
  • 6
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda, H., Arai, M., and Kuwajima, K. 2000. Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39: 12025-12032.
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 9
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. 2002. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 10
    • 0021070752 scopus 로고
    • Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent
    • Jones, W.J., Leigh, J.A., Mayer, F., Woese, C.R., and Wolfe, R.S. 1983. Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent. Arch. Microbiol. 136: 254-261.
    • (1983) Arch. Microbiol , vol.136 , pp. 254-261
    • Jones, W.J.1    Leigh, J.A.2    Mayer, F.3    Woese, C.R.4    Wolfe, R.S.5
  • 11
    • 13144276278 scopus 로고    scopus 로고
    • Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
    • Kim, R., Kim, K.K., Yokota, H., and Kim, S.H. 1998. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. 95: 9129-9133.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 9129-9133
    • Kim, R.1    Kim, K.K.2    Yokota, H.3    Kim, S.H.4
  • 12
    • 2142806742 scopus 로고    scopus 로고
    • Minimal protein-folding systems in hyperthermophilic archaea
    • Laksanalamai, P., Whitehead, T.A., and Robb, F.T. 2004. Minimal protein-folding systems in hyperthermophilic archaea. Nat. Rev. Microbiol. 2: 315-324.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 315-324
    • Laksanalamai, P.1    Whitehead, T.A.2    Robb, F.T.3
  • 13
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee, G.J., Pokala, N., and Vierling, E. 1995. Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol. Chem. 270: 10432-10438.
    • (1995) J. Biol. Chem , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 18
    • 0036299118 scopus 로고    scopus 로고
    • Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding
    • Okochi, M., Yoshida, T., Maruyama, T., Kawarabayasi, Y., Kikuchi, H., and Yohda, M. 2002. Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding. Biochem. Biophys. Res. Commun. 291: 769-774.
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 769-774
    • Okochi, M.1    Yoshida, T.2    Maruyama, T.3    Kawarabayasi, Y.4    Kikuchi, H.5    Yohda, M.6
  • 19
    • 3843093899 scopus 로고    scopus 로고
    • Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: Contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin
    • Okochi, M., Nomura, T., Zako, T., Arakawa, T., Iizuka, R., Ueda, H., Funatsu, T., Leroux, M., and Yohda, M. 2004. Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: Contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin. J. Biol. Chem. 279: 31788-31795.
    • (2004) J. Biol. Chem , vol.279 , pp. 31788-31795
    • Okochi, M.1    Nomura, T.2    Zako, T.3    Arakawa, T.4    Iizuka, R.5    Ueda, H.6    Funatsu, T.7    Leroux, M.8    Yohda, M.9
  • 20
    • 0036195309 scopus 로고    scopus 로고
    • Rupture of the cell envelope by decompression of the deep-sea methanogen Methanococcus jannaschii
    • Park, C.B. and Clark, D.S. 2002. Rupture of the cell envelope by decompression of the deep-sea methanogen Methanococcus jannaschii. Appl. Environ. Microbiol. 68: 1458-1463.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 1458-1463
    • Park, C.B.1    Clark, D.S.2
  • 22
    • 0036295232 scopus 로고    scopus 로고
    • Electron cryomicroscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum
    • Rockel, B., Jakana, J., Chiu, W., and Baumeister, W. 2002. Electron cryomicroscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum. J. Mol. Biol. 317: 673-681.
    • (2002) J. Mol. Biol , vol.317 , pp. 673-681
    • Rockel, B.1    Jakana, J.2    Chiu, W.3    Baumeister, W.4
  • 24
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Shao, Z.F., Mou, J., Czajkowsky, D.M., Yang, J., and Yuan, J.Y. 1996. Biological atomic force microscopy: What is achieved and what is needed. Adv. Phys. 45: 1-86.
    • (1996) Adv. Phys , vol.45 , pp. 1-86
    • Shao, Z.F.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.Y.5
  • 26
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M.R., Scheufler, C., Hartl, F.U., and Moarefi, I. 2000. Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103: 621-632.
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 29
    • 0032147230 scopus 로고    scopus 로고
    • Chaperonin filaments: Their formation and an evaluation of methods for studying them
    • Yaoi, T., Kagawa, H.K., and Trent, J.D. 1998. Chaperonin filaments: Their formation and an evaluation of methods for studying them. Arch. Biochem. Biophys. 356: 55-62.
    • (1998) Arch. Biochem. Biophys , vol.356 , pp. 55-62
    • Yaoi, T.1    Kagawa, H.K.2    Trent, J.D.3
  • 30
    • 33645217805 scopus 로고    scopus 로고
    • Selection of novel vesicular stomatitis virus glycoprotein variants from a peptide insertion library for enhanced purification of retroviral and lentiviral vectors
    • Yu, J.H. and Schaffer, D.V. 2006. Selection of novel vesicular stomatitis virus glycoprotein variants from a peptide insertion library for enhanced purification of retroviral and lentiviral vectors. J. Virol. 80: 3285-3292.
    • (2006) J. Virol , vol.80 , pp. 3285-3292
    • Yu, J.H.1    Schaffer, D.V.2
  • 31
    • 4444282445 scopus 로고    scopus 로고
    • Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis
    • Zhu, W., Reich, C.I., Olsen, G.J., Giometti, C.S., and Yates 3rd, J.R. 2004. Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis. J. Proteome Res. 3: 538-548.
    • (2004) J. Proteome Res , vol.3 , pp. 538-548
    • Zhu, W.1    Reich, C.I.2    Olsen, G.J.3    Giometti, C.S.4    Yates 3rd, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.