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Volumn 379, Issue 3, 1998, Pages 361-365

Prolyl isomerases do not catalyze isomerization of non-prolyl peptide bonds

Author keywords

Catalysis of folding; Cyclophilin; FKBP; Magnetization transfer; Parvulin; Protein folding; Trigger factor

Indexed keywords

CYCLOPHILIN; FK 506 BINDING PROTEIN; ISOMERASE; PROLINE DERIVATIVE; RIBONUCLEASE T1;

EID: 0031948782     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (49)
  • 1
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J.F., Halvorson, H.R., and Brennan, M. (1975). Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 2
    • 0028843879 scopus 로고
    • Calcineurin associated with the inositol 1,4,5- Trisphosphate receptor-FKBP12 complex modulates Ca2+ flux
    • Cameron, A.M., Steiner, J.P., Roskams, A.J., Ali, S.M., Ronnett, G. V., and Snyder, S.H. (1995). Calcineurin associated with the inositol 1,4,5-trisphosphate receptor-FKBP12 complex modulates Ca2+ flux. Cell 83, 463-472.
    • (1995) Cell , vol.83 , pp. 463-472
    • Cameron, A.M.1    Steiner, J.P.2    Roskams, A.J.3    Ali, S.M.4    Ronnett, G.V.5    Snyder, S.H.6
  • 3
    • 0004728957 scopus 로고
    • Fourier transform NMR pulse methods forthe measurement of slow-exchange rates
    • Campbell, D., Dobson, C.M., Ratcliffe, R.G., and Williams, R.J.P. (1978). Fourier transform NMR pulse methods forthe measurement of slow-exchange rates. J. Magn. Reson. 29, 397-417.
    • (1978) J. Magn. Reson. , vol.29 , pp. 397-417
    • Campbell, D.1    Dobson, C.M.2    Ratcliffe, R.G.3    Williams, R.J.P.4
  • 4
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FKBPs are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M.E., and Heitman, J. (1997). All cyclophilins and FKBPs are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc. Nat. Acad. Sci. USA 94, 13093-13098.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.E.3    Heitman, J.4
  • 5
    • 0028050923 scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and their effectors
    • Fischer, G. (1994). Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. 33, 1415-1436.
    • (1994) Angew. Chem. Int. Ed. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 6
    • 0021668676 scopus 로고
    • Nachweis einer Enzymkatalyse für die cis-trans-Isomerisierung der Peptid-bindung in prolinhaltigen Peptiden
    • Fischer, G., Bang, H., and Mech, C. (1984). Nachweis einer Enzymkatalyse für die cis-trans-Isomerisierung der Peptid-bindung in prolinhaltigen Peptiden. Biomed. Biochim. Acta 43, 1101-1111.
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 7
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E.K., Yuan, H.E.H., and Luban, J. (1994). Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372, 359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 9
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino- Terminal domain of HIV-1 capsid
    • Gamble, T.R., Vajdos, F.F., Yoo, S.H., Worthylake, D.K., Houseweart, M., Sundquist, W.I., and Hill, C.P. (1996). Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87, 1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.H.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 10
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C., and von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 11
    • 0029069724 scopus 로고
    • PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPlases
    • Hani, J., Stumpf, G., and Domdey, H. (1995). PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPlases. FEBS Lett. 365, 198-202.
    • (1995) FEBS Lett. , vol.365 , pp. 198-202
    • Hani, J.1    Stumpf, G.2    Domdey, H.3
  • 12
    • 0026055156 scopus 로고
    • Analysis of the steric strain in the polypeptide backbone of protein molecules
    • Herzberg, O., and Moult, J. (1991). Analysis of the steric strain in the polypeptide backbone of protein molecules. Proteins: Struct. Funct. Genet. 11, 223-229.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 13
    • 26044455503 scopus 로고
    • Cis-trans energy difference for the peptide bond in the gas phase and in aqueous solution
    • Jorgensen, W. L., and Gao, J. (1988). Cis-trans energy difference for the peptide bond in the gas phase and in aqueous solution. J. Am. Chem. Soc., 110, 4212-4216.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4212-4216
    • Jorgensen, W.L.1    Gao, J.2
  • 14
    • 0030876333 scopus 로고    scopus 로고
    • Rotational barriers of cis/trans isomerization of proline analogues and their catalysis of cyclophilin
    • Kern, D., Schutkowski, M., and Drakenberg, T. (1997). Rotational barriers of cis/trans isomerization of proline analogues and their catalysis of cyclophilin. J. Am. Chem. Soc. 119, 8403-8408.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8403-8408
    • Kern, D.1    Schutkowski, M.2    Drakenberg, T.3
  • 15
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S., and Baldwin, R.L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Ann. Rev. Biochem. 51, 459-489.
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 16
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S., and Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Ann. Rev. Biochem. 59, 631-660.
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 17
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang, K., Schmid, F.X., and Fischer, G. (1987). Catalysis of protein folding by prolyl isomerase. Nature 329, 268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 18
    • 0024285157 scopus 로고
    • Catalysis of proline isomerization during protein folding reactions
    • Lin, L.-N., Hasumi, H., and Brandts, J.F. (1988). Catalysis of proline isomerization during protein folding reactions. Biochim. Biophys. Acta 956, 256-266.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 256-266
    • Lin, L.-N.1    Hasumi, H.2    Brandts, J.F.3
  • 19
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K.P., Hanes, S.D., and Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 20
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • Macarthur, M.W., and Thornton, J.M. (1991). Influence of proline residues on protein conformation. J. Mol. Biol. 218, 397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • Macarthur, M.W.1    Thornton, J.M.2
  • 22
    • 0027250552 scopus 로고
    • Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine
    • Mayr, L.M., Landt, O., Hahn, U., and Schmid, F.X. (1993). Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine. J. Mol. Biol. 231, 897-912.
    • (1993) J. Mol. Biol. , vol.231 , pp. 897-912
    • Mayr, L.M.1    Landt, O.2    Hahn, U.3    Schmid, F.X.4
  • 23
    • 0027202274 scopus 로고
    • Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis proline 39 by alanine
    • Mayr, L.M., and Schmid, F.X. (1993a). Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis proline 39 by alanine. J. Mol. Biol. 231, 913-926.
    • (1993) J. Mol. Biol. , vol.231 , pp. 913-926
    • Mayr, L.M.1    Schmid, F.X.2
  • 24
    • 0027550008 scopus 로고
    • A purification method for labile variants of ribonuclease T1
    • Mayr, L. M., and Schmid, F. X. (1993b). A purification method for labile variants of ribonuclease T1. Protein Expression and Purification 4, 52-58.
    • (1993) Protein Expression and Purification , vol.4 , pp. 52-58
    • Mayr, L.M.1    Schmid, F.X.2
  • 25
    • 0028111284 scopus 로고
    • Generation of a non-prolyl cis peptide bond in ribonuclease T1
    • Mayr, L.M., Willbold, D., Rösch, P., and Schmid, F.X. (1994). Generation of a non-prolyl cis peptide bond in ribonuclease T1. J. Mol. Biol. 240, 288-293.
    • (1994) J. Mol. Biol. , vol.240 , pp. 288-293
    • Mayr, L.M.1    Willbold, D.2    Rösch, P.3    Schmid, F.X.4
  • 26
    • 0029868655 scopus 로고    scopus 로고
    • Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique
    • Mayr, L.M., Odefey, C., Schutkowski, M., and Schmid, F.X. (1996). Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry 35, 5550-5561.
    • (1996) Biochemistry , vol.35 , pp. 5550-5561
    • Mayr, L.M.1    Odefey, C.2    Schutkowski, M.3    Schmid, F.X.4
  • 27
    • 0026760365 scopus 로고
    • Enzymatic catalysis of prolyl isomerization in an unfolding protein
    • Mücke, M., and Schmid, F.X. (1992). Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry 37, 7848-7854.
    • (1992) Biochemistry , vol.37 , pp. 7848-7854
    • Mücke, M.1    Schmid, F.X.2
  • 28
    • 0028606121 scopus 로고
    • Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds
    • Mücke, M., and Schmid, F.X. (1994). Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry 33, 14608-14619.
    • (1994) Biochemistry , vol.33 , pp. 14608-14619
    • Mücke, M.1    Schmid, F.X.2
  • 29
    • 0028870213 scopus 로고
    • Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding
    • Odefey, C., Mayr, L.M., and Schmid, F.X. (1995). Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding. J. Mol. Biol. 245, 69-78.
    • (1995) J. Mol. Biol. , vol.245 , pp. 69-78
    • Odefey, C.1    Mayr, L.M.2    Schmid, F.X.3
  • 30
    • 0029101382 scopus 로고
    • The cyclosporin A-binding immunophilin Cyp-40 and the FK506- Binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor
    • Owens-Grillo, J.K., Hoffmann, K., Hutchison, K.A., Yem, A.W., Deibel, M.R., Handschumacher, R.E., and Pratt, W.B. (1995). The cyclosporin A-binding immunophilin Cyp-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor. J. Biol. Chem. 270, 20479-20484.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20479-20484
    • Owens-Grillo, J.K.1    Hoffmann, K.2    Hutchison, K.A.3    Yem, A.W.4    Deibel, M.R.5    Handschumacher, R.E.6    Pratt, W.B.7
  • 31
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli
    • Rahfeld, J.-U., Schierhorn, A., Mann, K.-H., and Fischer, G. (1994). A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett. 343, 65-69.
    • (1994) FEBS Lett. , vol.343 , pp. 65-69
    • Rahfeld, J.-U.1    Schierhorn, A.2    Mann, K.-H.3    Fischer, G.4
  • 32
    • 0017088666 scopus 로고
    • An explanation for the rare occurrence of cis peptide units in proteins and poly-peptides
    • Ramachandran, G. N., and Mitra, A. K. (1976). An explanation for the rare occurrence of cis peptide units in proteins and poly-peptides. J. Mol. Biol. 107, 85-92.
    • (1976) J. Mol. Biol. , vol.107 , pp. 85-92
    • Ramachandran, G.N.1    Mitra, A.K.2
  • 33
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan, R., Lu, K.P., Hunter, T., and Noel, J.P. (1997). Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89, 875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 34
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow, J., Mohrs, K., Koidl, S., Barthelmess, I.B., Pfanner, N., and Tropschug, M. (1995). Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell Biol. 15, 2654-2662.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 35
    • 0030931434 scopus 로고    scopus 로고
    • Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein
    • Reimer, U., Drewello, M., Jakob, M., Fischer, G., and Schutkowski, M. (1997). Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein. Biochem. J. 326, 181-185.
    • (1997) Biochem. J. , vol.326 , pp. 181-185
    • Reimer, U.1    Drewello, M.2    Jakob, M.3    Fischer, G.4    Schutkowski, M.5
  • 36
    • 0027256737 scopus 로고
    • Prolyl Isomerase - Enzymatic Catalysis of Slow Protein-Folding Reactions
    • Schmid, F.X. (1993). Prolyl Isomerase - Enzymatic Catalysis of Slow Protein-Folding Reactions. Ann. Rev. Biophys. Biomol. Struct. 22, 123-143.
    • (1993) Ann. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 123-143
    • Schmid, F.X.1
  • 38
    • 0029827590 scopus 로고    scopus 로고
    • Catalyzed and assisted protein folding of ribonuclease T1
    • Schmid, F.X., Frech, C., Scholz, C., and Walter, S. (1996). Catalyzed and assisted protein folding of ribonuclease T1. Biol. Chem. 377, 417-424.
    • (1996) Biol. Chem. , vol.377 , pp. 417-424
    • Schmid, F.X.1    Frech, C.2    Scholz, C.3    Walter, S.4
  • 40
    • 0030848403 scopus 로고    scopus 로고
    • Cyclophilin active-site mutants have native prolyl isomerase activity with a protein substrate
    • Scholz, C., Schindler, T., Dolinski, K., Heitman, J., and Schmid, F.X. (1997b). Cyclophilin active-site mutants have native prolyl isomerase activity with a protein substrate. FEBS Lett. 414, 69-73.
    • (1997) FEBS Lett. , vol.414 , pp. 69-73
    • Scholz, C.1    Schindler, T.2    Dolinski, K.3    Heitman, J.4    Schmid, F.X.5
  • 42
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive Ligands
    • Schreiber, S.L. (1991). Chemistry and biology of the immunophilins and their immunosuppressive Ligands. Science 251, 283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 43
    • 0027817195 scopus 로고
    • Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization
    • Stein, R.L. (1993). Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. Adv. Protein Chem. 44, 1-24.
    • (1993) Adv. Protein Chem. , vol.44 , pp. 1-24
    • Stein, R.L.1
  • 44
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Stewart, D.E., Sarkar, A., and Wampler, J.E. (1990). Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214, 253-260.
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 45
    • 0028864461 scopus 로고
    • Identification of the peptidyl-prolyl cis/trans isomerase bound to the Escherichia coli ribosome as the trigger factor
    • Stoller, G., Rücknagel, K.P., Nierhaus, K., Schmid, F.X., Fischer, G., and Rahfeld, J.-U. (1995). Identification of the peptidyl-prolyl cis/trans isomerase bound to the Escherichia coli ribosome as the trigger factor. EMBO J. 14, 4939-4948.
    • (1995) EMBO J. , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.-U.6
  • 46
    • 0014916912 scopus 로고
    • Ribonuclease T1: Structure and function
    • Takahashi, K., Uchida, T., and Egami, F. (1970). Ribonuclease T1: structure and function. Adv. Biophys. 1, 53-98.
    • (1970) Adv. Biophys. , vol.1 , pp. 53-98
    • Takahashi, K.1    Uchida, T.2    Egami, F.3
  • 49
    • 0031568329 scopus 로고    scopus 로고
    • Cyclophilin a complexed with a fragment of HIV-1 gag protein: Insights into HIV-1 infectious activity
    • Zhao, Y.D., Chen, Y.Q., Schutkowski, M., Fischer, G., and Ke, H.M. (1997). Cyclophilin A complexed with a fragment of HIV-1 gag protein: Insights into HIV-1 infectious activity. Structure 5, 139-146.
    • (1997) Structure , vol.5 , pp. 139-146
    • Zhao, Y.D.1    Chen, Y.Q.2    Schutkowski, M.3    Fischer, G.4    Ke, H.M.5


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