Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical

Journal of Biological Chemistry

Volumn 286, Issue 50, 2011, Pages 43447-43453

  Singarapu, Kiran K ^a   Tonelli, Marco ^a   Chow, Darius C ^a   Frederick, Ronnie O ^a   Westler, William M ^a   Markley, John L ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC; BIOPHYSICAL TECHNIQUES; CARBON-13; CIRCULAR DICHROISM SPECTRA; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 12; HETERONUCLEAR; LONG RANGE INTERACTIONS; MEMBRANE SURFACE; MEMBRANE-MIMETIC ENVIRONMENTS; NITROGEN-15; NMR SPECTRUM; PARAMAGNETIC SPINS; SDS MICELLES; SMALL HEAT SHOCK PROTEINS; STATIONARY PHASE; STRESS RESPONSE; STRUCTURAL CHARACTERIZATION; STRUCTURAL ELEMENTS;

CELL MEMBRANES; DICHROISM; DRIERS (MATERIALS); GADOLINIUM; MEMBRANES; MICELLES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMAGNETISM; SOLUTIONS; YEAST;

PROTEINS;

CARBON 13; DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 12; NITROGEN 15; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; PHOSPHORYLCHOLINE; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE PROTEINS; SODIUM DODECYL SULFATE;

EID: 83355163348     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.306464     Document Type: Article

References (35)

1. Craig, E. A. (1993) Science 260, 1902-1903
2. Hendrick, J. P., and Hartl, F. U. (1993) Annu. Rev. Biochem. 62, 349-384
3. Martin, J., and Hartl, F. U. (1997) Curr. Opin. Struct. Biol. 7, 41-52
4. Lindquist, S., and Craig, E. A. (1988) Annu. Rev. Genet. 22, 631-677
5. Schlesinger, M. J. (1990) J. Biol. Chem. 265, 12111-12114
6. Tissières, A., Mitchell, H. K., and Tracy, U. M. (1974) J. Mol. Biol. 84, 389-398
7. Praekelt, U. M., and Meacock, P. A. (1990) Mol. Gen. Genet. 223, 97-106
8. Stone, R. L., Matarese, V., Magee, B. B., Magee, P. T., and Bernlohr, D. A. (1990) Gene 96, 171-176
9. Mtwisha, L., Brandt, W., McCready, S., and Lindsey, G. G. (1998) Plant Mol. Biol. 37, 513-521
10. Sales, K., Brandt, W., Rumbak, E., and Lindsey, G. (2000) Bba Biomembranes 1463, 267-278
11. Motshwene, P., Karreman, R., Kgari, G., Brandt, W., and Lindsey, G. (2004) Biochem. J. 377, 769-774
12. Varela, J. C., Praekelt, U. M., Meacock, P. A., Planta, R. J., and Mager, W. H. (1995) Mol. Cell. Biol. 15, 6232-6245
13. Zara, S., Antonio Farris, G., Budroni, M., and Bakalinsky, A. T. (2002) Yeast 19, 269-276
14. Pacheco, A., Pereira, C., Almeida, M. J., and Sousa, M. J. (2009) Microbiology 155, 2021-2028
15. Schade, B., Jansen, G., Whiteway, M., Entian, K. D., and Thomas, D. Y. (2004) Mol. Biol. Cell 15, 5492-5502
16. Sano, F., Asakawa, N., Inoue, Y., and Sakurai, M. (1999) Cryobiology 39, 80-87
17. Park, J. I., Grant, C. M., Attfield, P. V., and Dawes, I. W. (1997) Appl. Environ. Microbiol. 63, 3818-3824
18. Sharma, S. C. (1997) FEMS Microbiol. Lett. 152, 11-15
19. Shamrock, V. J., and Lindsey, G. G. (2008) Can. J. Microbiol. 54, 559-568
20. Welker, S., Rudolph, B., Frenzel, E., Hagn, F., Liebisch, G., Schmitz, G., Scheuring, J., Kerth, A., Blume, A., Weinkauf, S., Haslbeck, M., Kessler, H., and Buchner, J. (2010) Mol. Cell 39, 507-520
21. Tyler, R. C., Sreenath, H. K., Singh, S., Aceti, D. J., Bingman, C. A., Markley, J. L., and Fox, B. G. (2005) Protein Expr. Purif. 40, 268-278
22. Sattler, M., Schleucher, J., and Griesinger, C. (1999) Prog. NMR Spectr. 34, 93-158
23. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293
24. Bartels, C., Xia, T. H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) J. Biomol. NMR 6, 1-10
25. Bahrami, A., Assadi, A. H., Markley, J. L., and Eghbalnia, H. R. (2009) PLoS Comput. Biol. 5, e1000307
26. Kay, L. E., Keifer, P., and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665
27. Farrow, N. A., Zhang, O., Forman-Kay, J. D., and Kay, L. E. (1995) Biochemistry 34, 868-878
28. Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) J. Biomol. NMR 44, 213-223
29. Güntert, P. (2004) Methods Mol. Biol. 278, 353-378
30. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graph. 14, 51-55
31. DeLano, W. L. (2010) The PyMOL Molecular Graphics System, version 1.3r1, Schrödinger, LLC, New York
32. Bhattacharya, A., Tejero, R., and Montelione, G. T. (2007) Proteins 66, 778-795
33. Hilty, C., Wider, G., Fernández, C., and Wüthrich, K. (2004) Chem. Bio. Chem. 5, 467-473
34. Laskowski, R. A., Rullmann, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
35. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) Nucleic Acids Res. 35, W375-383