메뉴 건너뛰기




Volumn 121, Issue 1, 1998, Pages 76-80

Purification, crystallization, and preliminary X-ray crystallographic data analysis of small heat shock protein homolog from Methanococcus jannaschii, a hyperthermophile

Author keywords

Hyperthermophile; Methanococcus jannaschii; Small heat shock protein; X ray crystallography

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 0031928719     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.3969     Document Type: Article
Times cited : (48)

References (22)
  • 1
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the Methanogenic Archaeon,Methanococcus jannaschii
    • Bult C. J., White O., Olsen G. J., Zhou L., Fleischmann R. D., Sutton G. G. Complete genome sequence of the Methanogenic Archaeon,Methanococcus jannaschii. Science. 273:1996;1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5    Sutton, G.G.6
  • 3
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family and structural predictions of the conserved "α-crystallin domain"
    • Caspers G-J., Leunissen J. A. M., de Jong W. W. The expanding small heat-shock protein family and structural predictions of the conserved "α-crystallin domain" Mol. Evol. 40:1995;238-248.
    • (1995) Mol. Evol. , vol.40 , pp. 238-248
    • Caspers, G-J.1    Leunissen, J.A.M.2    De Jong, W.W.3
  • 4
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis16-kDa antigen (Hsp16.3) functions as an oligomeric structurein vitroto suppress thermal aggregation
    • Chang Z., Primm T. P., Jakana J., Lee I. H., Serysheva I., Chium W., Gilbert H. F., Quiocho F. A. Mycobacterium tuberculosis16-kDa antigen (Hsp16.3) functions as an oligomeric structurein vitroto suppress thermal aggregation. J. Biol. Chem. 271:1996;7218-7223.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chium, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 6
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graber S., Gaestel M., Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16:1997;221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 7
    • 0027433255 scopus 로고
    • Heat shock and development induce synthesis of low- molecular-weight stress-responsive protein in the MyxobacteriumStigmatella aurantiaca
    • Heidelbach M., Skladny H., Schairer H. U. Heat shock and development induce synthesis of low- molecular-weight stress-responsive protein in the MyxobacteriumStigmatella aurantiaca. J. Bacteriol. 175:1993;7479-7482.
    • (1993) J. Bacteriol. , vol.175 , pp. 7479-7482
    • Heidelbach, M.1    Skladny, H.2    Schairer, H.U.3
  • 8
    • 0002561381 scopus 로고
    • How the protein folds in the cell
    • Oxford: IRL Press at Oxford Univ. Press. p. 194-228
    • Hlodan R., Hartl F. U. How the protein folds in the cell. Mechanisms of Protein Folding. 1994;IRL Press at Oxford Univ. Press, Oxford. p. 194-228.
    • (1994) Mechanisms of Protein Folding
    • Hlodan, R.1    Hartl, F.U.2
  • 9
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz J. α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 10
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jacob U., Gaestel M., Engel K., Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1993;1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jacob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 11
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik J., Kim S.-H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallog. 24:1991;409-411.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 12
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G. J., Roseman A. M., Saibil H. R., Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16:1997;659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 16
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallines modulates intermediate filament assembly
    • Nicholl I. D., Quinlan R. A. Chaperone activity of α-crystallines modulates intermediate filament assembly. EMBO J. 13:1994;945-953.
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 17
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precusor particles and are associated with a specific set of mRNAs
    • Nover L., Sharf K. D., Neumann D. Cytoplasmic heat shock granules are formed from precusor particles and are associated with a specific set of mRNAs. Mol. Cell. Biol. 9:1989;298-1308.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 298-1308
    • Nover, L.1    Sharf, K.D.2    Neumann, D.3
  • 18
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Data Collection and Processing. 1993;56-62 SERC Daresbury Laboratory, Warrington.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 19
    • 0028675582 scopus 로고
    • AnArabidopsisheat shock protein complements a thermotolerance defect in yeast
    • Schirmer E. C., Lindquist S., Vierling E. AnArabidopsisheat shock protein complements a thermotolerance defect in yeast. Plant Cell. 6:1994;1899-1909.
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1    Lindquist, S.2    Vierling, E.3
  • 21
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E. R., Lee J. L., Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47:1996;325-338.
    • (1996) J. Exp. Bot. , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, J.L.2    Vierling, E.3
  • 22
    • 0027229257 scopus 로고
    • Possible tetramer-based quaternary structures for α-crystallines and small heat shock proteins
    • Wistow G. Possible tetramer-based quaternary structures for α-crystallines and small heat shock proteins. Exp. Eye Res. 56:1993;729-732.
    • (1993) Exp. Eye Res. , vol.56 , pp. 729-732
    • Wistow, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.