메뉴 건너뛰기




Volumn 18, Issue 1, 2009, Pages 252-257

Mechanical unfolding of covalently linked GroES: Evidence of structural subunit intermediates

Author keywords

Covalently linked oligomeric protein; cpn10; Force spectroscopy; GroES; Mechanical unfolding intermediates; Protein subunit stability

Indexed keywords

CHAPERONIN; PROTEIN SUBUNIT;

EID: 58149476768     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.7     Document Type: Article
Times cited : (4)

References (28)
  • 1
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • Neet KE, Timm DE (1994) Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci 3:2167-2174.
    • (1994) Protein Sci , vol.3 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 2
    • 0029088389 scopus 로고
    • Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES
    • Zondlo J, Fisher KE, Lin Z, Ducote KR, Eisenstein E (1995) Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES. Biochemistry 34:10334-10339.
    • (1995) Biochemistry , vol.34 , pp. 10334-10339
    • Zondlo, J.1    Fisher, K.E.2    Lin, Z.3    Ducote, K.R.4    Eisenstein, E.5
  • 3
    • 0031563834 scopus 로고    scopus 로고
    • The structural stability of the co-chaperonin GroES
    • Boudker O, Todd MJ, Freire E (1997) The structural stability of the co-chaperonin GroES. J Mol Biol 272:770-779.
    • (1997) J Mol Biol , vol.272 , pp. 770-779
    • Boudker, O.1    Todd, M.J.2    Freire, E.3
  • 4
    • 0033588259 scopus 로고    scopus 로고
    • Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
    • Higurashi T, Nosaka K, Mizobata T, Nagai J, Kawata Y (1999) Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. J Mol Biol 291:703-713.
    • (1999) J Mol Biol , vol.291 , pp. 703-713
    • Higurashi, T.1    Nosaka, K.2    Mizobata, T.3    Nagai, J.4    Kawata, Y.5
  • 5
  • 6
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 7
    • 0141527459 scopus 로고    scopus 로고
    • Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering
    • Higurashi T, Hiragi Y, Ichimura K, Seki Y, Soda K, Mizobata T, Kawata Y (2003) Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. J Mol Biol 333:605-620.
    • (2003) J Mol Biol , vol.333 , pp. 605-620
    • Higurashi, T.1    Hiragi, Y.2    Ichimura, K.3    Seki, Y.4    Soda, K.5    Mizobata, T.6    Kawata, Y.7
  • 8
    • 0034489321 scopus 로고    scopus 로고
    • Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
    • Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P (2000) Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Protein Sci 9:2109-2117.
    • (2000) Protein Sci , vol.9 , pp. 2109-2117
    • Guidry, J.J.1    Moczygemba, C.K.2    Steede, N.K.3    Landry, S.J.4    Wittung-Stafshede, P.5
  • 9
    • 8544231377 scopus 로고    scopus 로고
    • Structural stability of oligomeric chaperonin 10: The role of two β-strands at the N and C termini in structural stabilization
    • Sakane I, Ikeda M, Matsumoto C, Higurashi T, Inoue K, Hongo K, Mizobata T, Kawata Y (2004) Structural stability of oligomeric chaperonin 10: the role of two β-strands at the N and C termini in structural stabilization. J Mol Biol 344:1123-1133.
    • (2004) J Mol Biol , vol.344 , pp. 1123-1133
    • Sakane, I.1    Ikeda, M.2    Matsumoto, C.3    Higurashi, T.4    Inoue, K.5    Hongo, K.6    Mizobata, T.7    Kawata, Y.8
  • 10
    • 27644534843 scopus 로고    scopus 로고
    • Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10
    • Luke K, Apiyo D, Wittung-Stafshede P (2005) Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10. Biochemistry 44:14385-14395.
    • (2005) Biochemistry , vol.44 , pp. 14385-14395
    • Luke, K.1    Apiyo, D.2    Wittung-Stafshede, P.3
  • 11
    • 0029665047 scopus 로고    scopus 로고
    • 2-macroglobulin molecules with atomic force microscope
    • 2-macroglobulin molecules with atomic force microscope. FEBS Lett 385:29-33.
    • (1996) FEBS Lett , vol.385 , pp. 29-33
    • Mitsui, K.1    Hara, M.2    Ikai, A.3
  • 13
    • 33846940059 scopus 로고    scopus 로고
    • Mechanical unfolding of proteins: Insights into biology, structure and folding
    • Forman JR, Clarke J (2007) Mechanical unfolding of proteins: insights into biology, structure and folding. Curr Opin Struct Biol 17:58-66.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 58-66
    • Forman, J.R.1    Clarke, J.2
  • 14
    • 33947098544 scopus 로고    scopus 로고
    • Structural stability of covalently linked GroES heptamer: Advantages in the formation of oligomeric structure
    • Sakane I, Hongo K, Motojima F, Murayama S, Mizobata T, Kawata Y (2007) Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure. J Mol Biol 367:1171-1185.
    • (2007) J Mol Biol , vol.367 , pp. 1171-1185
    • Sakane, I.1    Hongo, K.2    Motojima, F.3    Murayama, S.4    Mizobata, T.5    Kawata, Y.6
  • 15
    • 0035341202 scopus 로고    scopus 로고
    • Mediatorless biosensor for H2O2 based on recombinant forms of horseradish peroxidase directly adsorbed on polycrystalline gold
    • Ferapontova EE, Grigorenko VG, Egorov AM, Börchers T, Ruzgas T, Gorton L (2001) Mediatorless biosensor for H2O2 based on recombinant forms of horseradish peroxidase directly adsorbed on polycrystalline gold. Biosens Bioelectron 16:147-157.
    • (2001) Biosens Bioelectron , vol.16 , pp. 147-157
    • Ferapontova, E.E.1    Grigorenko, V.G.2    Egorov, A.M.3    Börchers, T.4    Ruzgas, T.5    Gorton, L.6
  • 16
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 17
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM (1998) The molecular elasticity of the extracellular matrix protein tenascin. Nature 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 22
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief M, Pascual J, Saraste M, Gaub HE (1999) Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J Mol Biol 286:553-561.
    • (1999) J Mol Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 23
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best RB, Li B, Steward A, Daggett V, Clarke J (2001) Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J 81:2344-2356.
    • (2001) Biophys J , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 24
    • 33751418948 scopus 로고    scopus 로고
    • Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability
    • Luke K, Wittung-Stafshede P (2006) Folding and assembly pathways of co-chaperonin proteins 10: origin of bacterial thermostability. Arch Biochem Biophys 456:8-18.
    • (2006) Arch Biochem Biophys , vol.456 , pp. 8-18
    • Luke, K.1    Wittung-Stafshede, P.2
  • 25
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
    • Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J (2002) Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J Mol Biol 322:841-849.
    • (2002) J Mol Biol , vol.322 , pp. 841-849
    • Fowler, S.B.1    Best, R.B.2    Toca Herrera, J.L.3    Rutherford, T.J.4    Steward, A.5    Paci, E.6    Karplus, M.7    Clarke, J.8
  • 27
    • 33749263567 scopus 로고    scopus 로고
    • Kinetic folding and assembly mechanisms differ for two homologous heptamers
    • Luke K, Perham M, Wittung-Stafshede P (2006) Kinetic folding and assembly mechanisms differ for two homologous heptamers. J Mol Biol 363:729-742.
    • (2006) J Mol Biol , vol.363 , pp. 729-742
    • Luke, K.1    Perham, M.2    Wittung-Stafshede, P.3
  • 28
    • 0026640258 scopus 로고
    • Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP
    • Mizobata T, Akiyama Y, Ito K, Yumoto N, Kawata Y (1992) Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP J Biol Chem 267:17773-17779.
    • (1992) J Biol Chem , vol.267 , pp. 17773-17779
    • Mizobata, T.1    Akiyama, Y.2    Ito, K.3    Yumoto, N.4    Kawata, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.