메뉴 건너뛰기




Volumn 64, Issue 4, 2007, Pages 917-922

Chaperoning Anfinsen: The steric foldases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEINASE; TRIACYLGLYCEROL LIPASE;

EID: 34248366452     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05718.x     Document Type: Short Survey
Times cited : (30)

References (39)
  • 1
    • 0036301647 scopus 로고    scopus 로고
    • The cold-active lipase of Pseudomonas fragi. Heterologous expression, biochemical characterization and molecular modeling
    • Alquati, C., De Gioia, L., Santarossa, G., Alberghina, L., Fantucci, P. Lotti, M. (2002) The cold-active lipase of Pseudomonas fragi. Heterologous expression, biochemical characterization and molecular modeling. Eur J Biochem 269 : 3321 3328.
    • (2002) Eur J Biochem , vol.269 , pp. 3321-3328
    • Alquati, C.1    De Gioia, L.2    Santarossa, G.3    Alberghina, L.4    Fantucci, P.5    Lotti, M.6
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science 181 : 223 230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0029645279 scopus 로고
    • Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 Å structure of the subtilisin- prodomain complex
    • Bryan, P., Wang, L., Hoskins, J., Ruvinov, S., Strausberg, S., Alexander, P., et al. (1995) Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin- prodomain complex. Biochemistry 34 : 10310 10318.
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P.1    Wang, L.2    Hoskins, J.3    Ruvinov, S.4    Strausberg, S.5    Alexander, P.6
  • 6
    • 0027483426 scopus 로고
    • Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson, K.W., Jacob-Dubuisson, F., Striker, R.T. Hultgren, S.J. (1993) Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc Natl Acad Sci USA 90 : 3670 3674.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3670-3674
    • Dodson, K.W.1    Jacob-Dubuisson, F.2    Striker, R.T.3    Hultgren, S.J.4
  • 7
    • 0027464607 scopus 로고
    • Folding of subtilisin BPN′: Characterization of a folding intermediate
    • Eder, J., Rheinnecker, M. Fersht, A.R. (1993) Folding of subtilisin BPN′: characterization of a folding intermediate. Biochemistry 32 : 18 26.
    • (1993) Biochemistry , vol.32 , pp. 18-26
    • Eder, J.1    Rheinnecker, M.2    Fersht, A.R.3
  • 8
    • 0032996078 scopus 로고    scopus 로고
    • Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor
    • El Khattabi, M., Ockhuijsen, C., Bitter, W., Jaeger, K.-E. Tommassen, J. (1999) Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor. Mol Gen Genet 261 : 770 776.
    • (1999) Mol Gen Genet , vol.261 , pp. 770-776
    • El Khattabi, M.1    Ockhuijsen, C.2    Bitter, W.3    Jaeger, K.-E.4    Tommassen, J.5
  • 9
    • 0034282656 scopus 로고    scopus 로고
    • Role of the lipase-specific foldase of Burkholderia glumae as a steric chaperone
    • El Khattabi, M., Van Gelder, P., Bitter, W. Tommassen, J. (2000) Role of the lipase-specific foldase of Burkholderia glumae as a steric chaperone. J Biol Chem 275 : 26885 26891.
    • (2000) J Biol Chem , vol.275 , pp. 26885-26891
    • El Khattabi, M.1    Van Gelder, P.2    Bitter, W.3    Tommassen, J.4
  • 10
    • 0038692116 scopus 로고    scopus 로고
    • Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase
    • El Khattabi, M., Van Gelder, P., Bitter, W. Tommassen, J. (2003) Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase. J Mol Catal, B Enzym 22 : 329 338.
    • (2003) J Mol Catal, B Enzym , vol.22 , pp. 329-338
    • El Khattabi, M.1    Van Gelder, P.2    Bitter, W.3    Tommassen, J.4
  • 11
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux, A. (2004) The underlying mechanisms of type II protein secretion. Biochim Biophys Acta 1694 : 163 179.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 12
    • 0027182430 scopus 로고
    • Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumae
    • Frenken, L.G.J., de Groot, A., Tommassen, J. Verrips, C.T. (1993) Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumae. Mol Microbiol 9 : 591 599.
    • (1993) Mol Microbiol , vol.9 , pp. 591-599
    • Frenken, L.G.J.1    De Groot, A.2    Tommassen, J.3    Verrips, C.T.4
  • 13
    • 2142715907 scopus 로고    scopus 로고
    • The 0.83 Å resolution crystal structure of α-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain
    • Fuhrmann, C.N., Kelch, B.A., Ota, N. Agard, D.A. (2004) The 0.83 Å resolution crystal structure of α-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain. J Mol Biol 338 : 999 1013.
    • (2004) J Mol Biol , vol.338 , pp. 999-1013
    • Fuhrmann, C.N.1    Kelch, B.A.2    Ota, N.3    Agard, D.A.4
  • 14
    • 0034718517 scopus 로고    scopus 로고
    • Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli
    • Hermanns, U., Sebbels, P., Eggli, V. Glockshuber, R. (2000) Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli. Biochemistry 39 : 11564 11570.
    • (2000) Biochemistry , vol.39 , pp. 11564-11570
    • Hermanns, U.1    Sebbels, P.2    Eggli, V.3    Glockshuber, R.4
  • 15
    • 0003742069 scopus 로고
    • London: Department of Biochemistry and Molecular biology. University College London.
    • Hubbard, S.J. Thornton, J.M. (1993) 'naccess', Computer Program. London : Department of Biochemistry and Molecular biology. University College London.
    • (1993) 'Naccess', Computer Program.
    • Hubbard, S.J.1    Thornton, J.M.2
  • 17
    • 0037122769 scopus 로고    scopus 로고
    • Energetic landscape of a-lytic protease optimizes longevity through kinetic stability
    • Jaswal, S.S., Sohl, J.L., Davis, J.H. Agard, D.A. (2002) Energetic landscape of a-lytic protease optimizes longevity through kinetic stability. Nature 415 : 343 346.
    • (2002) Nature , vol.415 , pp. 343-346
    • Jaswal, S.S.1    Sohl, J.L.2    Davis, J.H.3    Agard, D.A.4
  • 18
    • 14644412777 scopus 로고    scopus 로고
    • Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases
    • Jaswal, S.S., Trulhar, S.M.E., Dill, K.A. Agard, D.A. (2005) Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases. J Mol Biol 347 : 355 366.
    • (2005) J Mol Biol , vol.347 , pp. 355-366
    • Jaswal, S.S.1    Trulhar, S.M.E.2    Dill, K.A.3    Agard, D.A.4
  • 19
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones, C.H., Danese, P.N., Pinkner, J.S., Silhavy, T.J. Hultgren, S.J. (1997) The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J 16 : 6394 6406.
    • (1997) EMBO J , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 20
    • 0034811043 scopus 로고    scopus 로고
    • Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: Proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator
    • Kim, E.K., Jang, W.H., Ko, J.H., Kang, J.S., Noh, M.J. Yoo, O.J. (2001) Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator. J Bacteriol 183 : 5937 5941.
    • (2001) J Bacteriol , vol.183 , pp. 5937-5941
    • Kim, E.K.1    Jang, W.H.2    Ko, J.H.3    Kang, J.S.4    Noh, M.J.5    Yoo, O.J.6
  • 21
    • 11044223673 scopus 로고    scopus 로고
    • Identification of residues in the Pseudomonas aeruginosa propeptide required for chaperone and secretion activities
    • McIver, K.S., Kessler, E. Ohman, D.E. (2004) Identification of residues in the Pseudomonas aeruginosa propeptide required for chaperone and secretion activities. Microbiology 150 : 3969 3977.
    • (2004) Microbiology , vol.150 , pp. 3969-3977
    • McIver, K.S.1    Kessler, E.2    Ohman, D.E.3
  • 23
    • 0032169518 scopus 로고    scopus 로고
    • Pro-region C-terminus: Protease active site interactions are critical in catalyzing the folding of á-lytic protease
    • Peters, R.J., Shiau, A.K., Sohl, J.L., Anderson, D.E., Tang, G., Silen, J.L. Agard, D.A. (1998) Pro-region C-terminus: protease active site interactions are critical in catalyzing the folding of á-lytic protease. Biochemistry 37 : 12058 12067.
    • (1998) Biochemistry , vol.37 , pp. 12058-12067
    • Peters, R.J.1    Shiau, A.K.2    Sohl, J.L.3    Anderson, D.E.4    Tang, G.5    Silen, J.L.6    Agard, D.A.7
  • 25
    • 0031788058 scopus 로고    scopus 로고
    • Structure of α-lytic protease complexed with its pro region
    • Sauter, N.K., Mau, T., Rader, S.D. Agard, D.A. (1998) Structure of α-lytic protease complexed with its pro region. Nat Struct Biol 5 : 945 950.
    • (1998) Nat Struct Biol , vol.5 , pp. 945-950
    • Sauter, N.K.1    Mau, T.2    Rader, S.D.3    Agard, D.A.4
  • 26
    • 0031992088 scopus 로고    scopus 로고
    • Molecular properties and activity of amino-terminal truncated forms of lipase activator protein
    • Shibata, H., Kato, H. Oda, J. (1998a) Molecular properties and activity of amino-terminal truncated forms of lipase activator protein. Biosci Biotechnol Biochem 62 : 354 357.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 354-357
    • Shibata, H.1    Kato, H.2    Oda, J.3
  • 27
    • 0031847060 scopus 로고    scopus 로고
    • Random mutagenesis on the Pseudomonas lipase activator protein, LipB: Exploring amino acid residues required for its function
    • Shibata, H., Kato, H. Oda, J. (1998b) Random mutagenesis on the Pseudomonas lipase activator protein, LipB: exploring amino acid residues required for its function. Protein Eng 11 : 467 472.
    • (1998) Protein Eng , vol.11 , pp. 467-472
    • Shibata, H.1    Kato, H.2    Oda, J.3
  • 28
    • 0030756534 scopus 로고    scopus 로고
    • Protein memory through altered folding mediated by intramolecular chaperones
    • Shinde, U.P., Liu, J.J. Inouye, M. (1997) Protein memory through altered folding mediated by intramolecular chaperones. Nature 389 : 520 522.
    • (1997) Nature , vol.389 , pp. 520-522
    • Shinde, U.P.1    Liu, J.J.2    Inouye, M.3
  • 29
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of α-lytic protease are more stable than its native state
    • Sohl, J.L., Jaswal, S.S. Agard, D.A. (1998) Unfolded conformations of α-lytic protease are more stable than its native state. Nature 395 : 817 819.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 30
    • 33749538453 scopus 로고    scopus 로고
    • Convergent evolution of clamp-like binding sites in diverse chaperones
    • Stirling, P.C., Bakhoum, S.F., Feigl, A.B. Leroux, M.R. (2006) Convergent evolution of clamp-like binding sites in diverse chaperones. Nat Struct Mol Biol 13 : 865 870.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 865-870
    • Stirling, P.C.1    Bakhoum, S.F.2    Feigl, A.B.3    Leroux, M.R.4
  • 31
    • 14644437656 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Intrinsically unstructured propeptide modulates stochastic activation of subtilisin
    • Subbian, E., Yabuta, Y. Shinde, U.P. (2005) Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin. J Mol Biol 347 : 367 383.
    • (2005) J Mol Biol , vol.347 , pp. 367-383
    • Subbian, E.1    Yabuta, Y.2    Shinde, U.P.3
  • 33
    • 0036392235 scopus 로고    scopus 로고
    • Chaperone-independent folding of type 1 pilus domains
    • Vetsch, M., Sebbel, P. Glockshuber, R. (2002) Chaperone-independent folding of type 1 pilus domains. J Mol Biol 322 : 827 840.
    • (2002) J Mol Biol , vol.322 , pp. 827-840
    • Vetsch, M.1    Sebbel, P.2    Glockshuber, R.3
  • 35
    • 0032478201 scopus 로고    scopus 로고
    • Engineering the independent folding of the subtilisin BPN′ pro-domain: Correlation of pro-domain stability with the rate of subtilisin folding
    • Wang, L., Ruan, B., Ruvinov, S. Bryan, P.N. (1998) Engineering the independent folding of the subtilisin BPN′ pro-domain: correlation of pro-domain stability with the rate of subtilisin folding. Biochemistry 37 : 3165 3171.
    • (1998) Biochemistry , vol.37 , pp. 3165-3171
    • Wang, L.1    Ruan, B.2    Ruvinov, S.3    Bryan, P.N.4
  • 37
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak, S.J. Janin, J. (2002) Structural basis of macromolecular recognition. Adv Protein Chem 61 : 9 73.
    • (2002) Adv Protein Chem , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 38
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: Preserved folding energy drives fiber formation
    • Zavialov, A.V., Berglund, J., Pudney, A.F., Fooks, L.J., Ibrahim, T.M., MacIntyre, S. Knight, S.D. (2003) Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113 : 587 596.
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5    MacIntyre, S.6    Knight, S.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.