참고문헌
- Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181: 223-230. https://doi.org/10.1126/science.181.4096.223
- Gething MJ, Sambrook J. 1992. Protein folding in the cell. Nature 355: 33-45. https://doi.org/10.1038/355033a0
- Horwich AL, Fenton WA, Chapman E, Farr GW. 2007. Two families of chaperonin: physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23: 115-145. https://doi.org/10.1146/annurev.cellbio.23.090506.123555
- Hartl FU. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571-579. https://doi.org/10.1038/381571a0
- Ranson NA, White HE, Saibil HR. 1998. Chaperonins. J. Biochem. 33: 233-242. https://doi.org/10.1042/bj3330233
- Bukau B, Horwich AL. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366. https://doi.org/10.1016/S0092-8674(00)80928-9
- Ellis RH, Hartl FU. 1996. Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10: 20-26. https://doi.org/10.1096/fasebj.10.1.8566542
- Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858. https://doi.org/10.1126/science.1068408
- Hartl FU, Hayer-Hartl M. 2009. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16: 574-581. https://doi.org/10.1038/nsmb.1591
- Gutsche I, Essen LO, Baumeister W. 1999. Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. J. Mol. Biol. 293: 295-312. https://doi.org/10.1006/jmbi.1999.3008
- Reissmann S, Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J. 2012. A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Rep. 2: 866-877. https://doi.org/10.1016/j.celrep.2012.08.036
- Taro K, Ryo I, Kazunobu T, Kosuke M, Rie M, Muhamad S, et al. 2008. Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins. J. Biol. Chem. 50: 34773-34784.
- Ditzel L, Löwe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. 1998. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93: 125-138. https://doi.org/10.1016/S0092-8674(00)81152-6
- Shomura Y, Yoshida T, Iizuka R, Maruyama T, Yohda M, Miki K. 2004. Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms J. Mol. Biol. 335: 1265-1278. https://doi.org/10.1016/j.jmb.2003.11.028
- Xu Z, Horwich AL, Sigler PB. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388: 741-750. https://doi.org/10.1038/41944
- Horovitz A, Willison KR. 2005. Allosteric regulation of chaperonins. Curr. Opin. Struct. Biol. 15: 646-651. https://doi.org/10.1016/j.sbi.2005.10.001
- Yebenes H, Mesa P, Munoz IG, Montoya G, Valpuesta JM. 2011. Chaperonins: two rings for folding. Trends Biochem. Sci. 36: 424-432. https://doi.org/10.1016/j.tibs.2011.05.003
- Cong Y, Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, et al. 2010. 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc. Natl. Acad. Sci. USA 107: 4967-4972. https://doi.org/10.1073/pnas.0913774107
- Huo Y, Hu Z, Zhang K, Wang L, Zhai Y, Zhou Q, et al. 2010. Crystal structure of group II chaperonin in the open state. Structure 18: 1270-1279. https://doi.org/10.1016/j.str.2010.07.009
- Lopez T, Dalton K, Frydman J. 2015. The Mechanism and Function of Group II Chaperonins. J. Mol. Biol. 427: 2919-2930. https://doi.org/10.1016/j.jmb.2015.04.013
- Meyer AS, Gillespie JR, Walther D, Millet IS, Doniach S, Frydman J. 2003. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113: 369-381. https://doi.org/10.1016/S0092-8674(03)00307-6
- Galit K, Keith RW, Amnon H. 2001. Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1. Prot. Sci. 10: 445-449. https://doi.org/10.1110/ps.44401
- Kim JH, Shin EJ, Jeon SJ, Kim YH, Kim P, Lee CH, Nam SW. 2009. Overexpression, purification, and functional characterization of the group ІІ chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3. Biotechnol. Bioprocess Eng. 14: 551-558. https://doi.org/10.1007/s12257-009-0008-0
- Geladopoulos TP, Sotiroudis TG, Evangelopoulos AE. 1991. A malachite green colorimetric assay for protein phosphatase activity. Anal. Biochem. 192: 112-116. https://doi.org/10.1016/0003-2697(91)90194-X
- Okochi M, Matsuzaki H, Nomura T, Ishii N, Yohda M. 2005. Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3. Extremophiles 9: 127-134. https://doi.org/10.1007/s00792-004-0427-y
- Viitanen PV, Lubben TH, Reed J, Goloubinoff P, O'Keefe DP, Lorimer GH. 1990. Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent. Biochemistry 29: 5665-5671. https://doi.org/10.1021/bi00476a003
- Guagliardi A, Cerchia L, Bartolucci S, Rossi M. 1994. The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro. Protein Sci. 3: 1436-1443. https://doi.org/10.1002/pro.5560030910
- Gutsche I, Mihalache O, Baumeister W. 2000. ATPase cycle of an archaeal chaperonin. J. Mol. Biol. 300: 187-196. https://doi.org/10.1006/jmbi.2000.3833
- Chen HY, Tan XL, Lu J, Zhang CX, Zhang Y, Yang SL. 2009. Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus. Biotechnol. Lett. 31: 1753-1758. https://doi.org/10.1007/s10529-009-0070-x
- Russell R, Jordan R, McMacken R. 1998. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone. Biochemistry 37: 596-607. https://doi.org/10.1021/bi972025p
- Silberg JJ, Vickery LE. 2000. Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 275: 7779-7786. https://doi.org/10.1074/jbc.275.11.7779