메뉴 건너뛰기




Volumn 20, Issue 3, 2010, Pages 542-549

Overexpression, purification, and characterization of β-subunit of group ii chaperonin from hyperthermophilic aeropyrum pernix K1

Author keywords

Aeropyrum pernix; Alcohol dehydrogenase; ATPase activity; Chaperonin; Citrate synthase; Malate dehydrogenase; Pro carboxypeptidase B

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALCOHOL DEHYDROGENASE; CHAPERONIN; CHAPERONIN B; CITRATE SYNTHASE; MALATE DEHYDROGENASE; PEPTIDE HYDROLASE; PROCARBOXYPEPTIDASE B; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77954303953     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0909.09025     Document Type: Article
Times cited : (2)

References (37)
  • 1
    • 0030031369 scopus 로고    scopus 로고
    • Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri
    • Andra, S., G. Frey, M. Nitsch, W. Baumeister, and K. O. Stetter. 1996. Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri. FEBS Lett. 379: 127-131.
    • (1996) FEBS Lett , vol.379 , pp. 127-131
    • Andra, S.1    Frey, G.2    Nitsch, M.3    Baumeister, W.4    Stetter, K.O.5
  • 5
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii
    • Bult, C. J., O. White, G. J. Olsen, L. Zhou, R. D. Fleischmann, G. G. Sutton, et al. 1996. Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii. Science 273: 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
  • 6
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang, Z., T. Primm, J. Jakana, I. H. Lee, I. Serysheva, W. Chiu, H. F. Gilbert, and F. A. Cuiocho. 1996. Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 271: 7218-7223.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Cuiocho, F.A.8
  • 7
    • 33646692199 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a hyperalkaline phosphatase from the thermophilic bacterium Thermus sp. T351
    • Choi, J. J., J. W. Park, H. K. Shim, S. C. Lee, M. S. Kwon, J. S. Yang, H. O. Hwang, and S. T. Kwon. 2006. Cloning, expression, and characterization of a hyperalkaline phosphatase from the thermophilic bacterium Thermus sp. T351. J. Microbiol. Biotechnol. 16: 272-279.
    • (2006) J. Microbiol. Biotechnol. , vol.16 , pp. 272-279
    • Choi, J.J.1    Park, J.W.2    Shim, H.K.3    Lee, S.C.4    Kwon, M.S.5    Yang, J.S.6    Hwang, H.O.7    Kwon, S.T.8
  • 8
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., J. Lowe, D. Stock, K. O. Stetter, H. Huber, R. Huber, and S. Steinbacher. 1998. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93: 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 9
    • 0032561205 scopus 로고    scopus 로고
    • Group II chaperonin in a thermophilic methanogen Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability
    • Furutani, M., T. Iida, T. Yoshida, and T. Maruyama. 1998. Group II chaperonin in a thermophilic methanogen Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability. J. Biol. Chem. 273: 28399-28407.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28399-28407
    • Furutani, M.1    Iida, T.2    Yoshida, T.3    Maruyama, T.4
  • 10
    • 18144383544 scopus 로고    scopus 로고
    • Refolding and purification of recombinant human interferon-γ expressed as inclusion bodies in Escherichia coli using size exclusion chromatography
    • Guan, Y. X., H. X. Pan, Y. G. Gao, S. J. Yao, and M. G. Cho. 2005. Refolding and purification of recombinant human interferon-γ expressed as inclusion bodies in Escherichia coli using size exclusion chromatography. Biotechnol. Bioprocess Eng. 10: 122-127.
    • (2005) Biotechnol. Bioprocess Eng. , vol.10 , pp. 122-127
    • Guan, Y.X.1    Pan, H.X.2    Gao, Y.G.3    Yao, S.J.4    Cho, M.G.5
  • 11
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • Gutsche, I., L. O. Essen, and W. Baumeister. 1999. Group II chaperonins: New TRiC(k)s and turns of a protein folding machine. J. Mol. Biol. 293: 295-312.
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3
  • 12
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 13
    • 0842328576 scopus 로고    scopus 로고
    • Identification of a redox-regulated chaperone network
    • Hoffmann, J. H., K. Linke, P. C. Graf, H. Lilie, and U. Jakob. 2004. Identification of a redox-regulated chaperone network. EMBO J. 23: 160-168.
    • (2004) EMBO J , vol.23 , pp. 160-168
    • Hoffmann, J.H.1    Linke, K.2    Graf, P.C.3    Lilie, H.4    Jakob, U.5
  • 14
    • 0032937393 scopus 로고    scopus 로고
    • Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-deficient mutant enzyme
    • Isumi, M., S. Fuiwara, M. Takagi, S. Kanaya, and T. Imanaka. 1999. Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-deficient mutant enzyme. Appl. Environ. Microbiol. 65: 1801-1805.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1801-1805
    • Isumi, M.1    Fuiwara, S.2    Takagi, M.3    Kanaya, S.4    Imanaka, T.5
  • 15
    • 0033616977 scopus 로고    scopus 로고
    • Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1
    • Kawarabayasi, Y., Y. Hino, H. Horikawa, S. Yamazaki, Y. Haikawa, K. Jin-no, et al. 1999. Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1. DNA Res. 6: 83-101, 145-152.
    • (1999) DNA Res , vol.6
    • Kawarabayasi, Y.1    Hino, Y.2    Horikawa, H.3    Yamazaki, S.4    Haikawa, Y.5    Jin-No, K.6
  • 16
    • 30344454674 scopus 로고    scopus 로고
    • Refolding of fusion ferritin by gel filtration chromatography (GFC)
    • Kim, H. and I. H. Kim. 2005. Refolding of fusion ferritin by gel filtration chromatography (GFC). Biotechnol. Bioprocess Eng. 10: 500-504.
    • (2005) Biotechnol. Bioprocess Eng. , vol.10 , pp. 500-504
    • Kim, H.1    Kim, I.H.2
  • 17
    • 0027992757 scopus 로고
    • Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
    • Kim, S., K. R. Willson, and A. L. Horwich. 1994. Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem. Sci. 19: 543-548.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 543-548
    • Kim, S.1    Willson, K.R.2    Horwich, A.L.3
  • 18
    • 0028116350 scopus 로고
    • The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus. A biochemical and structural characterization
    • Knapp, S., I. Schhmidt-Krey, H. Hebert, T. Bergman, H. Jornvall, and R. Ladenstein. 1994. The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus. A biochemical and structural characterization. J. Mol. Biol. 242: 397-407.
    • (1994) J. Mol. Biol. , vol.242 , pp. 397-407
    • Knapp, S.1    Schhmidt-Krey, I.2    Hebert, H.3    Bergman, T.4    Jornvall, H.5    Ladenstein, R.6
  • 19
    • 33745669745 scopus 로고    scopus 로고
    • Stabilization of free and immobilized enzyme using hyperthermophilic chaperonin
    • Kohda, J., H. Kawanishi, K. Suehara, Y. Nakano, and T. Yano. 2006. Stabilization of free and immobilized enzyme using hyperthermophilic chaperonin. J. Biosci. Bioeng. 101: 131-136.
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 131-136
    • Kohda, J.1    Kawanishi, H.2    Suehara, K.3    Nakano, Y.4    Yano, T.5
  • 20
    • 0036161561 scopus 로고    scopus 로고
    • Improvement of productivity of active form of glutamate racemase in Escherichia coli by coexpression of folding accessory proteins
    • Kohda, J., Y. Endo, N. Okumura, Y. Kurokawa, K. Nishihara, H. Yanagi, T. Yura, H. Fukuda, and A. Kondo. 2002. Improvement of productivity of active form of glutamate racemase in Escherichia coli by coexpression of folding accessory proteins. Biochem. Eng. J. 10: 39-45.
    • (2002) Biochem. Eng. J. , vol.10 , pp. 39-45
    • Kohda, J.1    Endo, Y.2    Okumura, N.3    Kurokawa, Y.4    Nishihara, K.5    Yanagi, H.6    Yura, T.7    Fukuda, H.8    Kondo, A.9
  • 21
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1) multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota, H., G. Hynes, and K. Willson. 1995. The chaperonin containing t-complex polypeptide 1 (TCP-1) multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur. J. Biochem. 230: 3-16.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willson, K.3
  • 23
    • 0037000608 scopus 로고    scopus 로고
    • Overproduction of Bacillus macerans cyclodextrin glucanotransferase in E. coli by coexpression of GroEL/ES chaperone
    • Kwon, M. J., S. L. Rark, S. K. Kim, and S. W. Nam. 2002. Overproduction of Bacillus macerans cyclodextrin glucanotransferase in E. coli by coexpression of GroEL/ES chaperone. J. Microbiol. Biotechnol. 12: 1002-1005.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 1002-1005
    • Kwon, M.J.1    Rark, S.L.2    Kim, S.K.3    Nam, S.W.4
  • 25
    • 0027092285 scopus 로고
    • Chaperonin mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., G. Pfeifer, J. Martin, W. Baumeister, and F. U. Hartl. 1992. Chaperonin mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11: 4757-4765.
    • (1992) EMBO J , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.U.5
  • 27
    • 0032401547 scopus 로고    scopus 로고
    • Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro
    • Minuth, T., G. Frey, P. Lindner, R. Rachel, K. O. Stetter, and R. Jaenicke. 1998. Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro. Eur. J. Biochem. 258: 837-845.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 837-845
    • Minuth, T.1    Frey, G.2    Lindner, P.3    Rachel, R.4    Stetter, K.O.5    Jaenicke, R.6
  • 28
    • 33845546523 scopus 로고    scopus 로고
    • Properties of the α subunit of a chaperonin from the hyperthermophilic crenarchaeon Aeropyrum pernix K1
    • Son, H. J., E. J. Shin, S. W. Nam, D. E. Kim, and S. J. Jeon. 2006. Properties of the α subunit of a chaperonin from the hyperthermophilic crenarchaeon Aeropyrum pernix K1. FEMS Microbiol. Lett. 266: 103-109.
    • (2006) FEMS Microbiol. Lett. , vol.266 , pp. 103-109
    • Son, H.J.1    Shin, E.J.2    Nam, S.W.3    Kim, D.E.4    Jeon, S.J.5
  • 29
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilicarchaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J. D., E. Nimmesgern, J. S. Wall, F. U. Hartl, and A. L. Horwich. 1991. A molecular chaperone from a thermophilicarchaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354: 490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 30
    • 0028814839 scopus 로고
    • The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC
    • Waldmann, T., E. Nimmesgern, M. Nitsch, J. Peters, G. Pfeifer, S. Muller, et al. 1995. The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. Eur. J. Biochem. 227: 848-856.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 848-856
    • Waldmann, T.1    Nimmesgern, E.2    Nitsch, M.3    Peters, J.4    Pfeifer, G.5    Muller, S.6
  • 31
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • Wiech, H., J. Buchner, R. Zimmermann, and U. Jakob. 1992. Hsp90 chaperones protein folding in vitro. Nature 358: 169-170.
    • (1992) Nature , vol.358 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 32
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • Winter, J., K. Linke, A. Jatzek, and U. Jakob. 2005. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol. Cell. 17: 381-392.
    • (2005) Mol. Cell. , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 33
    • 0030953876 scopus 로고    scopus 로고
    • In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1
    • Yan, Z., S. Fujiwara, K. Kohda, M. Takagi, and T. Imanaka. 1997. In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1. Appl. Environ. Microbiol. 63: 785-789.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 785-789
    • Yan, Z.1    Fujiwara, S.2    Kohda, K.3    Takagi, M.4    Imanaka, T.5
  • 34
    • 0031592944 scopus 로고    scopus 로고
    • Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1
    • Yoshida, T., M. Yohda, T. Iida, T. Maruyama, H. Taguchi, K. Yazaki, et al. 1997. Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1. J. Mol. Biol. 273: 635-645.
    • (1997) J. Mol. Biol. , vol.273 , pp. 635-645
    • Yoshida, T.1    Yohda, M.2    Iida, T.3    Maruyama, T.4    Taguchi, H.5    Yazaki, K.6
  • 35
    • 0036290267 scopus 로고    scopus 로고
    • Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin
    • Yoshida, T., R. Kawaguchi, H. Taguchi, M. Yoshida, T. Wakabayashi, M. Yohda, and T. Maruyama. 2002. Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin. J. Mol. Biol. 315: 73-85.
    • (2002) J. Mol. Biol. , vol.315 , pp. 73-85
    • Yoshida, T.1    Kawaguchi, R.2    Taguchi, H.3    Yoshida, M.4    Wakabayashi, T.5    Yohda, M.6    Maruyama, T.7
  • 36
    • 0026058532 scopus 로고
    • Conformational stability of pig citrate synthase and some active-site mutants
    • Zhi, W., P. Srere, and C. T. Evans. 1991. Conformational stability of pig citrate synthase and some active-site mutants. Biochemistry 30: 9281-9286.
    • (1991) Biochemistry , vol.30 , pp. 9281-9286
    • Zhi, W.1    Srere, P.2    Evans, C.T.3
  • 37
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: Influence of denaturant and folding assistants
    • Zhi, W., S. J. Landry, L. M. Gierasch, and P. A. Srere. 1992. Renaturation of citrate synthase: Influence of denaturant and folding assistants. Prot. Sci. 1: 522-529.
    • (1992) Prot. Sci. , vol.1 , pp. 522-529
    • Zhi, W.1    Landry, S.J.2    Gierasch, L.M.3    Srere, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.