Effect of temperature and denaturation conditions on protein folding assisted by GroEL-GroES chaperonin |
Bae, Yu-Jin
(Department of Biomaterial Control (BK21 program), Dong-Eui University)
Jang, Kyoung-Jin (Department of Biomaterial Control (BK21 program), Dong-Eui University) Jeon, Sung-Jong (Department of Biomaterial Control (BK21 program), Dong-Eui University, Department of Biotechnology & Bioengineering, Dong-Eui University) Nam, Soo-Wan (Department of Biomaterial Control (BK21 program), Dong-Eui University, Department of Biotechnology & Bioengineering, Dong-Eui University) Lee, Jae-Hyung (Department of Biomaterial Control (BK21 program), Dong-Eui University, Department of Biotechnology & Bioengineering, Dong-Eui University) Kim, Young-Man (Department of Food and Nutrition/Oriental Biotech Co., Dong-Eui University) Kim, Dong-Eun (Department of Biomaterial Control (BK21 program), Dong-Eui University, Department of Biotechnology & Bioengineering, Dong-Eui University) |
1 | Srere, P. A. 1966. Citrate-condensing enzyme-oxalacetate binary complex. Studies on its physical and chemical properties. J. Biol. Chem. 241, 2157-2165 |
2 | Viitanen, P. V., C. K. Donaldson, C. H. Lorimer, T. H. Lubben and A. A. Gatenby. 1991. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry. 30, 9716-9723 DOI ScienceOn |
3 | Zhi, W., P. Srere and C. T. Evans. 1991. Conformational stability of pig citrate synthase and some active-site mutants. Biochemistry. 30, 9281-9286 DOI ScienceOn |
4 | Horwich, A. L., K. B. Low, W. A Fenton, I. N. Hirshfield and K. Furtak. 1993. Folding in vivo of bacterial cytoplasmic pruteins: role of GroEL. Cell. 74, 909-917 DOI ScienceOn |
5 | Mendoza, J. A., G. H. Lorimer and P. M. Horowitz. 1992. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures. J. Biol. Chem. 267, 17631-17634 |
6 | Laminet, A. A., T. Ziegelhoffer, C. Georgopoulos and A. Pluckthun. 1990. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9, 2315-2319 |
7 | Lorimer, G. H. 1996. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. J. FASEB. 10, 5-9 DOI |
8 | Martin, J., A. L. Horwich and F. U. Hartl. 1992. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science. 258, 995-998 DOI |
9 | Mendoza, J. A., E. Rogers, G. H. Lorimer and P. M. Horowitz. 1991. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem. 266, 13044-13049 |
10 | Morimoto, R. I., A Tissieres and C. Georgopoulos. 1994. The biology of heat shock proteins and molecular chperones. Cold Spring Harbor Press, New York |
11 | Panda, M., B. M. Gorovits and P. M. Horowitz. 2000. Productive and nonproductive intermediates in the folding of denatured rhodanese. J. Biol. Chem. 275, 63-70 DOI ScienceOn |
12 | Ptitsyn, O. B. 1992. in protein Folding (Creighton, T. E., ed) pp 243-300, W. H. Freeman and Co., New York |
13 | Schmidt, M., J. Buchner, M. J. Todd, G. H. Lorimer and P. V. Viitanen. 1994. On the role of groES in the chaperonin-assisted folding reaction: Three case studies. J. Biol. Chem. 269, 10304-10311 |
14 | Ewbank, J. J. and T. E. Creighton. 1991. The molten globule protein conformation probed by disulphide bonds. Nature. 350, 518-520 DOI ScienceOn |
15 | Bhattacharyya, A. M. and P. M. Horowitz. 2001. The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation. J. Biol. Chem. 276, 28739-28743 DOI ScienceOn |
16 | Buchner, J., M. Schmidt, M. Fuchs, R. Jaenicke, R. Rudolph, F. X. Schmid and T. Kiefhaber. 1991. GruE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30, 1586-1591 DOI ScienceOn |
17 | Ewalt, K. L., J. P. Hendrick, W. A. Houry and F. U. Hartl. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90, 491-500 DOI ScienceOn |
18 | Fenton, W. A., Y. Kashi, K. Furtak and A. L. Horwich. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371, 614-619 DOI ScienceOn |
19 | Goloubinoff, P., S. Diamant, C. Weiss and A Azem. 1997. GruES binding regulates GroEL chaperunin activity under heat shock. FEBS Lett. 407, 215-219 DOI ScienceOn |
20 | Grallert, H. and J. Buchner. 1999. Analysis of GroE-assisted folding under nonpermissive conditions. J. Biol. Chem. 274, 20171-20177 DOI |
21 | Holl-Neugebauer, B., R. Rudolph, M. Schmidt and J. Buchner. 1991. Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast. Biochemistry. 30, 11609-11614 DOI ScienceOn |
22 | Horowitz, P. M. and N. L. Criscimagna. 1990. Stable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese. J. Biol. Chem. 265, 2576-2583 |
23 | Fayet, O., T. Ziegelhoffer and C. Georgopoulos. 1989. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385 DOI |