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

Journal of Structural Biology

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

  Kim, Kyeong Kyu ^a   Yokota, Hisao ^a   Santoso, Steve ^a   Lerner, Dimitry ^a   Kim, Rosalind ^a   Kim, Sung Hou ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

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

Indexed keywords

HEAT SHOCK PROTEIN;

ARTICLE; CRYSTALLIZATION; METHANOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PURIFICATION; X RAY CRYSTALLOGRAPHY;

ARCHAEA; ESCHERICHIA COLI; METHANOBACTERIUM; METHANOCALDOCOCCUS JANNASCHII; METHANOCOCCUS; TRIXIS;

EID: 0031928719     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.3969     Document Type: Article

References (22)

1. 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.
2. 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.
3. 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.
4. 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.
5. Acta Crystallogr. Section D. 50:1994;760-763.
6. 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.
7. 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.
8. 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.
9. Horwitz J. α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
10. Jacob U., Gaestel M., Engel K., Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1993;1517-1520.
11. Jancarik J., Kim S.-H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallog. 24:1991;409-411.
12. 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.
13. Merck K. B., Groenen P. J., Voorter C. E., de Haard-Hoekman W. A., Horwitz J., Bloemendal H., de Jong W. W. Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. J. Biol. Chem. 268:1993;1046-1052.
14. Miron T., Vancompernolle K., Vanderkerchhove J., Wilchek M., Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J. Cell. Biol. 114:1991;255-261.
15. Morimoto R., Tissieres A., Georgopolous C. The Biology of Heat Shock Proteins and Molecular Chaperones. 1994;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
16. Nicholl I. D., Quinlan R. A. Chaperone activity of α-crystallines modulates intermediate filament assembly. EMBO J. 13:1994;945-953.
17. 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.
18. Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Data Collection and Processing. 1993;56-62 SERC Daresbury Laboratory, Warrington.
19. Schirmer E. C., Lindquist S., Vierling E. AnArabidopsisheat shock protein complements a thermotolerance defect in yeast. Plant Cell. 6:1994;1899-1909.
20. van den Ijssel P. R., Overkamp P., Knauf U., Gaestel M., de Jong W. W. α-crystallin confers cellular thermoresistance. FEBS. Lett. 355:1994;54-56.
21. 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.
22. Wistow G. Possible tetramer-based quaternary structures for α-crystallines and small heat shock proteins. Exp. Eye Res. 56:1993;729-732.