메뉴 건너뛰기




Volumn 396, Issue 5, 2010, Pages 1271-1283

Characterisation of a GroEL Single-Ring Mutant that Supports Growth of Escherichia coli and Has GroES-Dependent ATPase Activity

Author keywords

Allostery; Chaperonin; GroEL; Single ring

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONIN;

EID: 77649274107     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.11.074     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet O., Ziegelhoffer T., Georgopoulos C. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 1989, 171:1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 3
    • 33750489742 scopus 로고    scopus 로고
    • Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL
    • Chapman E., Farr G.W., Usaite R., Furtak K., Fenton W.A., Chaudhuri T.K., et al. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc. Natl Acad. Sci. USA 2006, 103:15800-15805.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15800-15805
    • Chapman, E.1    Farr, G.W.2    Usaite, R.3    Furtak, K.4    Fenton, W.A.5    Chaudhuri, T.K.6
  • 5
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 1996, 379:37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 6
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 9
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 1994, 371:614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 10
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
    • Chen L., Sigler P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell 1999, 99:757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 11
    • 19844377583 scopus 로고    scopus 로고
    • The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy
    • Falke S., Tama F., Brooks C.L., Gogol E.P., Fisher M.T. The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy. J. Mol. Biol. 2005, 348:219-230.
    • (2005) J. Mol. Biol. , vol.348 , pp. 219-230
    • Falke, S.1    Tama, F.2    Brooks, C.L.3    Gogol, E.P.4    Fisher, M.T.5
  • 12
    • 40949124274 scopus 로고    scopus 로고
    • GroEL stimulates protein folding through forced unfolding
    • Lin Z., Madan D., Rye H.S. GroEL stimulates protein folding through forced unfolding. Nat. Struct. Mol. Biol. 2008, 15:303-311.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 303-311
    • Lin, Z.1    Madan, D.2    Rye, H.S.3
  • 13
    • 4944221602 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: making the impossible, possible
    • Lin Z., Rye H.S. GroEL-mediated protein folding: making the impossible, possible. Mol. Cell 2004, 16:23-34.
    • (2004) Mol. Cell , vol.16 , pp. 23-34
    • Lin, Z.1    Rye, H.S.2
  • 14
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
    • Todd M.J., Viitanen P.V., Lorimer G.H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 1994, 265:659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 15
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman J.S., Kashi Y., Fenton W.A., Horwich A.L. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 1994, 78:693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 16
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston S.G., Ranson N.A., Clarke A.R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 1995, 249:138-152.
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 17
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 1996, 84:481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 20
    • 58149229533 scopus 로고    scopus 로고
    • Chaperonin complex with a newly folded protein encapsulated in the folding chamber
    • Clare D.K., Bakkes P.J., van Heerikhuizen H., van der Vies S.M., Saibil H.R. Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature 2009, 457:107-110.
    • (2009) Nature , vol.457 , pp. 107-110
    • Clare, D.K.1    Bakkes, P.J.2    van Heerikhuizen, H.3    van der Vies, S.M.4    Saibil, H.R.5
  • 21
    • 33746357595 scopus 로고    scopus 로고
    • Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE
    • Cliff M.J., Limpkin C., Cameron A., Burston S.G., Clarke A.R. Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. J. Biol. Chem. 2006, 281:21266-21275.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21266-21275
    • Cliff, M.J.1    Limpkin, C.2    Cameron, A.3    Burston, S.G.4    Clarke, A.R.5
  • 22
  • 23
    • 0029087065 scopus 로고
    • Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
    • Ranson N.A., Dunster N.J., Burston S.G., Clarke A.R. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 1995, 250:581-586.
    • (1995) J. Mol. Biol. , vol.250 , pp. 581-586
    • Ranson, N.A.1    Dunster, N.J.2    Burston, S.G.3    Clarke, A.R.4
  • 24
    • 56249135270 scopus 로고    scopus 로고
    • Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
    • Apetri A.C., Horwich A.L. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc. Natl Acad. Sci. USA 2008, 105:17351-17355.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 17351-17355
    • Apetri, A.C.1    Horwich, A.L.2
  • 25
    • 0037062480 scopus 로고    scopus 로고
    • Simulations of beta-hairpin folding confined to spherical pores using distributed computing
    • Klimov D.K., Newfield D., Thirumalai D. Simulations of beta-hairpin folding confined to spherical pores using distributed computing. Proc. Natl Acad. Sci. USA 2002, 99:8019-8024.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8019-8024
    • Klimov, D.K.1    Newfield, D.2    Thirumalai, D.3
  • 26
    • 34547507851 scopus 로고    scopus 로고
    • Effects of crowding and confinement on the structures of the transition state ensemble in proteins
    • Cheung M.S., Thirumalai D. Effects of crowding and confinement on the structures of the transition state ensemble in proteins. J. Phys. Chem. B 2007, 111:8250-8257.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 8250-8257
    • Cheung, M.S.1    Thirumalai, D.2
  • 28
    • 33646897305 scopus 로고    scopus 로고
    • Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    • Tang Y.C., Chang H.C., Roeben A., Wischnewski D., Wischnewski N., Kerner M.J., et al. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 2006, 125:903-914.
    • (2006) Cell , vol.125 , pp. 903-914
    • Tang, Y.C.1    Chang, H.C.2    Roeben, A.3    Wischnewski, D.4    Wischnewski, N.5    Kerner, M.J.6
  • 29
    • 68649123756 scopus 로고    scopus 로고
    • The GroEL/GroES cis cavity as a passive anti-aggregation device
    • Horwich A.L., Apetri A.C., Fenton W.A. The GroEL/GroES cis cavity as a passive anti-aggregation device. FEBS Lett. 2009, 583:2654-2662.
    • (2009) FEBS Lett. , vol.583 , pp. 2654-2662
    • Horwich, A.L.1    Apetri, A.C.2    Fenton, W.A.3
  • 30
    • 0141754010 scopus 로고    scopus 로고
    • Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    • Chaudhry C., Farr G.W., Todd M.J., Rye H.S., Brunger A.T., Adams P.D., et al. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J. 2003, 22:4877-4887.
    • (2003) EMBO J. , vol.22 , pp. 4877-4887
    • Chaudhry, C.1    Farr, G.W.2    Todd, M.J.3    Rye, H.S.4    Brunger, A.T.5    Adams, P.D.6
  • 31
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye H.S., Roseman A.M., Chen S., Furtak K., Fenton W.A., Saibil H.R., Horwich A.L. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 1999, 97:325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 32
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 1996, 87:241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 33
    • 0035715944 scopus 로고    scopus 로고
    • Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding
    • Saibil H.R., Horwich A.L., Fenton W.A. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Adv. Protein Chem. 2001, 59:45-72.
    • (2001) Adv. Protein Chem. , vol.59 , pp. 45-72
    • Saibil, H.R.1    Horwich, A.L.2    Fenton, W.A.3
  • 34
    • 45649083920 scopus 로고    scopus 로고
    • Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET
    • Papo N., Kipnis Y., Haran G., Horovitz A. Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET. J. Mol. Biol. 2008, 380:717-725.
    • (2008) J. Mol. Biol. , vol.380 , pp. 717-725
    • Papo, N.1    Kipnis, Y.2    Haran, G.3    Horovitz, A.4
  • 35
    • 0028135063 scopus 로고
    • Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala
    • Yifrach O., Horovitz A. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala. J. Mol. Biol. 1994, 243:397-401.
    • (1994) J. Mol. Biol. , vol.243 , pp. 397-401
    • Yifrach, O.1    Horovitz, A.2
  • 36
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 1995, 34:5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 37
    • 0028785583 scopus 로고
    • Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES
    • Weissman J.S., Hohl C.M., Kovalenko O., Kashi Y., Chen S., Braig K., et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 1995, 83:577-587.
    • (1995) Cell , vol.83 , pp. 577-587
    • Weissman, J.S.1    Hohl, C.M.2    Kovalenko, O.3    Kashi, Y.4    Chen, S.5    Braig, K.6
  • 38
    • 0033575308 scopus 로고    scopus 로고
    • Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form
    • Erbse A., Yifrach O., Jones S., Lund P.A. Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form. J. Biol. Chem. 1999, 274:20351-20357.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20351-20357
    • Erbse, A.1    Yifrach, O.2    Jones, S.3    Lund, P.A.4
  • 40
    • 0032113635 scopus 로고    scopus 로고
    • A single ring is sufficient for productive chaperonin-mediated folding in vivo
    • Nielsen K.L., Cowan N.J. A single ring is sufficient for productive chaperonin-mediated folding in vivo. Mol. Cell 1998, 2:93-99.
    • (1998) Mol. Cell , vol.2 , pp. 93-99
    • Nielsen, K.L.1    Cowan, N.J.2
  • 41
    • 0034671453 scopus 로고    scopus 로고
    • From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL
    • Chatellier J., Hill F., Foster N.W., Goloubinoff P., Fersht A.R. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL. J. Mol. Biol. 2000, 304:897-910.
    • (2000) J. Mol. Biol. , vol.304 , pp. 897-910
    • Chatellier, J.1    Hill, F.2    Foster, N.W.3    Goloubinoff, P.4    Fersht, A.R.5
  • 42
    • 0042736829 scopus 로고    scopus 로고
    • Isolation and characterisation of mutants of GroEL that are fully functional as single rings
    • Sun Z., Scott D.J., Lund P.A. Isolation and characterisation of mutants of GroEL that are fully functional as single rings. J. Mol. Biol. 2003, 332:715-728.
    • (2003) J. Mol. Biol. , vol.332 , pp. 715-728
    • Sun, Z.1    Scott, D.J.2    Lund, P.A.3
  • 43
    • 0025995773 scopus 로고
    • Cooperativity in ATP hydrolysis by GroEL is increased by GroES
    • Gray T.E., Fersht A.R. Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 1991, 292:254-258.
    • (1991) FEBS Lett. , vol.292 , pp. 254-258
    • Gray, T.E.1    Fersht, A.R.2
  • 45
    • 2142814279 scopus 로고    scopus 로고
    • A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL
    • Poso D., Clarke A.R., Burston S.G. A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL. J. Mol. Biol. 2004, 338:969-977.
    • (2004) J. Mol. Biol. , vol.338 , pp. 969-977
    • Poso, D.1    Clarke, A.R.2    Burston, S.G.3
  • 46
    • 0030846353 scopus 로고    scopus 로고
    • Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37°C but not at 43°C
    • Ivic A., Olden D., Wallington E.J., Lund P.A. Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37°C but not at 43°C. Gene 1997, 194:1-8.
    • (1997) Gene , vol.194 , pp. 1-8
    • Ivic, A.1    Olden, D.2    Wallington, E.J.3    Lund, P.A.4
  • 47
    • 2142822809 scopus 로고    scopus 로고
    • Kinetic analysis of ATP-dependent inter-ring communication in GroEL
    • Amir A., Horovitz A. Kinetic analysis of ATP-dependent inter-ring communication in GroEL. J. Mol. Biol. 2004, 338:979-988.
    • (2004) J. Mol. Biol. , vol.338 , pp. 979-988
    • Amir, A.1    Horovitz, A.2
  • 48
    • 0030995661 scopus 로고    scopus 로고
    • Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
    • Behlke J., Ristau O., Schonfeld H.J. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry 1997, 36:5149-5156.
    • (1997) Biochemistry , vol.36 , pp. 5149-5156
    • Behlke, J.1    Ristau, O.2    Schonfeld, H.J.3
  • 49
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding
    • Jackson G.S., Staniforth R.A., Halsall D.J., Atkinson T., Holbrook J.J., Clarke A.R., Burston S.G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 1993, 32:2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 50
    • 0027250447 scopus 로고
    • Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion
    • Todd M.J., Viitanen P.V., Lorimer G.H. Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry 1993, 32:8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 51
    • 0028609655 scopus 로고
    • Residue lysine-34 in GroES modulates allosteric transitions in GroEL
    • Kovalenko O., Yifrach O., Horovitz A. Residue lysine-34 in GroES modulates allosteric transitions in GroEL. Biochemistry 1994, 33:14974-14978.
    • (1994) Biochemistry , vol.33 , pp. 14974-14978
    • Kovalenko, O.1    Yifrach, O.2    Horovitz, A.3
  • 52
    • 4644274961 scopus 로고    scopus 로고
    • Identification of a major inter-ring coupling step in the GroEL reaction cycle
    • Poso D., Clarke A.R., Burston S.G. Identification of a major inter-ring coupling step in the GroEL reaction cycle. J. Biol. Chem. 2004, 279:38111-38117.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38111-38117
    • Poso, D.1    Clarke, A.R.2    Burston, S.G.3
  • 53
    • 0032546571 scopus 로고    scopus 로고
    • Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
    • Yifrach O., Horovitz A. Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry 1998, 37:7083-7088.
    • (1998) Biochemistry , vol.37 , pp. 7083-7088
    • Yifrach, O.1    Horovitz, A.2
  • 54
    • 0037436402 scopus 로고    scopus 로고
    • Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy
    • Inobe T., Arai M., Nakao M., Ito K., Kamagata K., Makio T., et al. Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J. Mol. Biol. 2003, 327:183-191.
    • (2003) J. Mol. Biol. , vol.327 , pp. 183-191
    • Inobe, T.1    Arai, M.2    Nakao, M.3    Ito, K.4    Kamagata, K.5    Makio, T.6
  • 55
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • Wang J.D., Herman C., Tipton K.A., Gross C.A., Weissman J.S. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 2002, 111:1027-1039.
    • (2002) Cell , vol.111 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4    Weissman, J.S.5
  • 56
    • 34248349952 scopus 로고    scopus 로고
    • Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
    • Farr G.W., Fenton W.A., Horwich A.L. Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc. Natl Acad. Sci. USA 2007, 104:5342-5347.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5342-5347
    • Farr, G.W.1    Fenton, W.A.2    Horwich, A.L.3
  • 58
    • 2642659387 scopus 로고    scopus 로고
    • GroE is vital for cell-wall synthesis
    • McLennan N., Masters M. GroE is vital for cell-wall synthesis. Nature 1998, 392:139.
    • (1998) Nature , vol.392 , pp. 139
    • McLennan, N.1    Masters, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.