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Volumn 150, Issue 4, 2011, Pages 403-409

StHsp14.0, a small heat shock protein of Sulfolobus tokodaii strain 7, protects denatured proteins from aggregation in the partially dissociated conformation

Author keywords

assembly and dissociation; chaperone; small angle X ray scattering; small heat shock protein; Sulfolobus tokodaii

Indexed keywords

CHAPERONE; CITRATE SYNTHASE; DIMER; OLIGOMER; SMALL HEAT SHOCK PROTEIN;

EID: 80053558864     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr074     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • DOI 10.1128/MMBR.66.1.64-93.2002
    • Narberhaus, F. (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66, 64-93 (Pubitemid 34213969)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.1 , pp. 64-93
    • Narberhaus, F.1
  • 2
    • 0027985159 scopus 로고
    • αA-crystallin confers cellular thermoresistance
    • DOI 10.1016/0014-5793(94)01175-3
    • Van den IJssel, P.R., Overkamp, P., Knauf, U., Gaestel, M., and de Jong, W.W (1994) Alpha A-crystallin confers cellular thermoresistance. FEBS Lett. 355, 54-56 (Pubitemid 24352102)
    • (1994) FEBS Letters , vol.355 , Issue.1 , pp. 54-56
    • Van Den Ijssel, P.R.L.A.1
  • 3
    • 0029001772 scopus 로고
    • Disruption of the gene for hsp30, an alpha-crystallin-related heat shock protein of Neurospora crassa, causes defects in thermotolerance
    • Plesofsky-Vig, N. and Brambl, R (1995) Disruption of the gene for hsp30, an alpha-crystallin-related heat shock protein of Neurospora crassa, causes defects in thermotolerance. Proc. Natl Acad. Sci. USA 92, 5032-5036
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5032-5036
    • Plesofsky-Vig, N.1    Brambl, R.2
  • 4
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz, J (1992) Alpha-crystallin can function as a molecular chaperone. Proc. Natl Acad. Sci. USA 89, 10449-10453
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 7
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain"
    • Caspers, G.J., Leunissen, J.A., and de Jong, W.W (1995) The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain". J. Mol. Evol. 40, 238-248
    • (1995) J. Mol. Evol. , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.2    De Jong, W.W.3
  • 10
    • 0031897554 scopus 로고    scopus 로고
    • Purification and characterization of small heat shock proteins
    • DOI 10.1016/S0076-6879(98)90030-1
    • Buchner, J., Ehrnsperger, M., Gaestel, M., and Walke, S (1998) Purification and characterization of small heat shock proteins. Methods Enzymol. 290, 339-349 (Pubitemid 28157762)
    • (1998) Methods in Enzymology , vol.290 , pp. 339-349
    • Buchner, J.1    Ehrnsperger, M.2    Gaestel, M.3    Walke, S.4
  • 11
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • DOI 10.1038/29106
    • Kim, K.K., Kim, R., and Kim, S.H (1998) Crystal structure of a small heat-shock protein. Nature 394, 595-599 (Pubitemid 28366837)
    • (1998) Nature , vol.394 , Issue.6693 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 13
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of α-crystallins: Alternative interactions and oligomeric assemblies
    • Pasta, S.Y., Raman, B., Ramakrishna, T., and Rao Ch, M (2004) The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies. Mol. Vis. 10, 655-662 (Pubitemid 41358231)
    • (2004) Molecular Vision , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, Ch.M.4
  • 14
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • DOI 10.1074/jbc.M407236200
    • Shashidharamurthy, R., Koteiche, H.A., Dong, J., and McHaourab, H.S (2005) Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J. Biol. Chem. 280, 5281-5289 (Pubitemid 40280001)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    Mchaourab, H.S.4
  • 15
    • 0032898210 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity
    • Yang, H., Huang, S., Dai, H., Gong, Y., Zheng, C., and Chang, Z (1999) The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity. Protein Sci. 8, 174-179 (Pubitemid 29035530)
    • (1999) Protein Science , vol.8 , Issue.1 , pp. 174-179
    • Yang, H.1    Huang, S.2    Dai, H.3    Gong, Y.4    Zheng, C.5    Chang, Z.6
  • 16
    • 33846018601 scopus 로고    scopus 로고
    • The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity
    • DOI 10.1074/jbc.M607677200
    • Basha, E., Friedrich, K.L., and Vierling, E (2006) The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity. J. Biol. Chem. 281, 39943-39952 (Pubitemid 46041798)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 39943-39952
    • Basha, E.1    Friedrich, K.L.2    Vierling, E.3
  • 17
    • 25444478296 scopus 로고    scopus 로고
    • Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature
    • DOI 10.1074/jbc.M504121200
    • Hirose, M., Tohda, H., Giga-Hama, Y., Tsushima, R., Zako, T., Iizuka, R., Pack, C., Kinjo, M., Ishii, N., and Yohda, M (2005) Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature. J. Biol. Chem. 280, 32586-3259318. (Pubitemid 41368300)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.38 , pp. 32586-32593
    • Hirose, M.1    Tohda, H.2    Giga-Hama, Y.3    Tsushima, R.4    Zako, T.5    Iizuka, R.6    Pack, C.7    Kinjo, M.8    Ishii, N.9    Yohda, M.10
  • 18
    • 21744436278 scopus 로고    scopus 로고
    • The activation mechanism of Hsp26 does not require dissociation of the oligomer
    • DOI 10.1016/j.jmb.2005.05.034, PII S0022283605005772
    • Franzmann, T.M., Wuhr, M., Richter, K., Walter, S., and Buchner, J (2005) The activation mechanism of Hsp26 does not require dissociation of the oligomer. J. Mol. Biol. 350, 1083-1093 (Pubitemid 40943464)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 1083-1093
    • Franzmann, T.M.1    Wuhr, M.2    Richter, K.3    Walter, S.4    Buchner, J.5
  • 19
    • 0347994114 scopus 로고    scopus 로고
    • Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7
    • DOI 10.1110/ps.03264204
    • Usui, K., Ishii, N., Kawarabayasi, Y., and Yohda, M (2004) Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7. Protein Sci. 13, 134-144 (Pubitemid 38021148)
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 134-144
    • Usui, K.1    Ishii, N.2    Kawarabayasi, Y.3    Yohda, M.4
  • 20
    • 41149087881 scopus 로고    scopus 로고
    • Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7
    • DOI 10.1002/prot.21762
    • Saji, H., Iizuka, R., Yoshida, T., Abe, T., Kidokoro, S., Ishii, N., and Yohda, M (2008) Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7. Proteins 71, 771-782 (Pubitemid 351430015)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.2 , pp. 771-782
    • Saji, H.1    Iizuka, R.2    Yoshida, T.3    Abe, T.4    Kidokoro, S.-I.5    Ishii, N.6    Yohda, M.7
  • 21
    • 85012257250 scopus 로고    scopus 로고
    • Present status of BL40B2 and BL40XU at SPring-8 (beamlines for small angle X-ray scattering)
    • Inoue, K., Oka, T., Miura, K., and Yagi, N (2004) Present Status of BL40B2 and BL40XU at SPring-8 (Beamlines for Small Angle X-ray Scattering). AIP Conf. Proc. 705, 336-339
    • (2004) AIP Conf. Proc. , vol.705 , pp. 336-339
    • Inoue, K.1    Oka, T.2    Miura, K.3    Yagi, N.4
  • 23
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D. and Svergun, D.I (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Cryst. 42, 342-346
    • (2009) J. Appl. Cryst. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 24
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V. and Svergun, D.I (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Cryst. 36, 860-864
    • (2003) J. Appl. Cryst. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 25
    • 0029881549 scopus 로고    scopus 로고
    • Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules
    • DOI 10.1006/jsbi.1996.0025
    • Yasunaga, T. and Wakabayashi, T (1996) Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules. J. Struct. Biol. 116, 155-160 (Pubitemid 26093138)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 155-160
    • Yasunaga, T.1    Wakabayashi, T.2
  • 27
    • 79952452537 scopus 로고    scopus 로고
    • Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0
    • Takeda, K., Hayashi, T., Abe, T., Hirano, Y., Hanazono, Y., Yohda, M., and Miki, K (2010) Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0. J. Struct. Biol. 174, 92-99
    • (2010) J. Struct. Biol. , vol.174 , pp. 92-99
    • Takeda, K.1    Hayashi, T.2    Abe, T.3    Hirano, Y.4    Hanazono, Y.5    Yohda, M.6    Miki, K.7
  • 28
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from x-ray solution scattering
    • DOI 10.1107/S0021889801012869
    • Wriggers, W. and Chacon, P (2001) Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering. J. Appl. Cryst. 34, 773-776 (Pubitemid 33144106)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.6 , pp. 773-776
    • Wriggers, W.1    Chacon, P.2


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