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Volumn 326, Issue 4, 2003, Pages 1189-1201

Solution structure of the cytotoxic RNase 4 from oocytes of bullfrog Rana catesbeiana

Author keywords

Antitumor; Cytotoxicity; NMR; Ribonuclease; Solution structure

Indexed keywords

GLUTAMINE; GUANIDINE; PANCREATIC RIBONUCLEASE; PYROGLUTAMIC ACID; RANPIRNASE; RECOMBINANT RNA;

EID: 0037470596     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01472-9     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 0034326938 scopus 로고    scopus 로고
    • Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog)
    • Liao Y.D., Huang H.C., Leu Y.J., Wei C.W., Tang P.C., Wang S.C. Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog). Nucl. Acids Res. 28:2000;4097-4104.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 4097-4104
    • Liao, Y.D.1    Huang, H.C.2    Leu, Y.J.3    Wei, C.W.4    Tang, P.C.5    Wang, S.C.6
  • 2
    • 0035006458 scopus 로고    scopus 로고
    • Rapid diversification of RNase A superfamily ribonucleases from the bullfrog Rana catesbeiana
    • Rosenberg H.F., Zhang J., Liao Y.D., Dyer K.D. Rapid diversification of RNase A superfamily ribonucleases from the bullfrog Rana catesbeiana. J. Mol. Evol. 53:2001;31-38.
    • (2001) J. Mol. Evol. , vol.53 , pp. 31-38
    • Rosenberg, H.F.1    Zhang, J.2    Liao, Y.D.3    Dyer, K.D.4
  • 4
    • 0031596225 scopus 로고    scopus 로고
    • G1 arrest of U937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation
    • Juan G., Ardelt B., Li X., Mikulski S.M., Shogen K., Ardelt W., et al. G1 arrest of U937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation. Leukemia. 12:1998;1241-1248.
    • (1998) Leukemia , vol.12 , pp. 1241-1248
    • Juan, G.1    Ardelt, B.2    Li, X.3    Mikulski, S.M.4    Shogen, K.5    Ardelt, W.6
  • 5
    • 0029871341 scopus 로고    scopus 로고
    • Role of the N terminus in RNase A homologues: Differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
    • Boix E., Wu Y., Vasandani V.M., Saxena S.K., Ardelt W., Ladner J., Youle R.J. Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity. J. Mol. Biol. 257:1996;992-1007.
    • (1996) J. Mol. Biol. , vol.257 , pp. 992-1007
    • Boix, E.1    Wu, Y.2    Vasandani, V.M.3    Saxena, S.K.4    Ardelt, W.5    Ladner, J.6    Youle, R.J.7
  • 6
    • 0024206672 scopus 로고
    • Expression of Met-(-1) angiogenin in Escherichia coli: Conversion to the authentic less than Glu-1 protein
    • Shapiro R., Harper J.W., Fox E.A., Jansen H.W., Hein F., Uhlmann E. Expression of Met-(-1) angiogenin in Escherichia coli: conversion to the authentic less than Glu-1 protein. Anal. Biochem. 175:1988;450-461.
    • (1988) Anal. Biochem. , vol.175 , pp. 450-461
    • Shapiro, R.1    Harper, J.W.2    Fox, E.A.3    Jansen, H.W.4    Hein, F.5    Uhlmann, E.6
  • 8
    • 0034625439 scopus 로고    scopus 로고
    • Conformational stability is a determinant of ribonuclease A cytotoxicity
    • Klink T.A., Raines R.T. Conformational stability is a determinant of ribonuclease A cytotoxicity. J. Biol. Chem. 275:2000;17463-17467.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17463-17467
    • Klink, T.A.1    Raines, R.T.2
  • 10
    • 0027256672 scopus 로고
    • A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity
    • Wu Y., Mikulski S.M., Ardelt W., Rybak S.M., Youle R.J. A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity. J. Biol. Chem. 268:1993;10686-10693.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10686-10693
    • Wu, Y.1    Mikulski, S.M.2    Ardelt, W.3    Rybak, S.M.4    Youle, R.J.5
  • 11
    • 0026758678 scopus 로고
    • In vivo and in vitro growth-inhibitory effect of bovine seminal ribonuclease on a system of rat thyroid epithelial transformed cells and tumors
    • Laccetti P., Portella G., Mastronicola M.R., Russo A., Piccoli R., D'Alessio G., Vecchio G. In vivo and in vitro growth-inhibitory effect of bovine seminal ribonuclease on a system of rat thyroid epithelial transformed cells and tumors. Cancer Res. 52:1992;4582-4586.
    • (1992) Cancer Res. , vol.52 , pp. 4582-4586
    • Laccetti, P.1    Portella, G.2    Mastronicola, M.R.3    Russo, A.4    Piccoli, R.5    D'Alessio, G.6    Vecchio, G.7
  • 12
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe B., Deisenhofer J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature. 374:1995;183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 13
    • 0035900671 scopus 로고    scopus 로고
    • Endowing human pancreatic ribonuclease with toxicity for cancer cells
    • Leland P.A., Staniszewski K.E., Kim B.M., Raines R.T. Endowing human pancreatic ribonuclease with toxicity for cancer cells. J. Biol. Chem. 276:2001;43095-43102.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43095-43102
    • Leland, P.A.1    Staniszewski, K.E.2    Kim, B.M.3    Raines, R.T.4
  • 14
    • 0023631047 scopus 로고
    • Ribonuclease structure and catalysis: Crystal structure of sulfate-free native ribonuclease A at 1.5-Å resolution
    • Campbell R.L., Petsko G.A. Ribonuclease structure and catalysis: crystal structure of sulfate-free native ribonuclease A at 1.5-Å resolution. Biochemistry. 26:1987;8579-8584.
    • (1987) Biochemistry , vol.26 , pp. 8579-8584
    • Campbell, R.L.1    Petsko, G.A.2
  • 16
    • 0030917539 scopus 로고    scopus 로고
    • Crystal structures of ribonuclease A complexes with 5′-diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 Å resolution
    • Leonidas D.D., Hapiro R., Irons L.I., Russo N., Acharya K.R. Crystal structures of ribonuclease A complexes with 5′-diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 Å resolution. Biochemistry. 36:1997;5578-5588.
    • (1997) Biochemistry , vol.36 , pp. 5578-5588
    • Leonidas, D.D.1    Hapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 17
    • 0025993410 scopus 로고
    • Novel non-productively bound ribonuclease inhibitor complexes - High resolution X-ray refinement studies on the binding of RNase-A to cytidylyl-2′,5′-guanosine (2′,5′CpG) and deoxy-cytidylyl-3′,5′-guanosine (3′,5′dCpdG)
    • Aguilar C.F., Thomas P.J., Moss D.S., Mills A., Palmer R.A. Novel non-productively bound ribonuclease inhibitor complexes - high resolution X-ray refinement studies on the binding of RNase-A to cytidylyl-2′,5′-guanosine (2′,5′CpG) and deoxy-cytidylyl-3′,5′-guanosine (3′,5′dCpdG). Biochim. Biophys. Acta. 1118:1991;6-20.
    • (1991) Biochim. Biophys. Acta , vol.1118 , pp. 6-20
    • Aguilar, C.F.1    Thomas, P.J.2    Moss, D.S.3    Mills, A.4    Palmer, R.A.5
  • 18
    • 0027511809 scopus 로고
    • High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy
    • Santoro J., Gonzalez C., Bruix M., Neira J.L., Nieto J.L., Herranz J., Rico M. High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 229:1993;722-734.
    • (1993) J. Mol. Biol. , vol.229 , pp. 722-734
    • Santoro, J.1    Gonzalez, C.2    Bruix, M.3    Neira, J.L.4    Nieto, J.L.5    Herranz, J.6    Rico, M.7
  • 19
    • 0030018454 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexes of ribonuclease A with 2′,5′-CpA and 3′,5′-d(CpA) in aqueous solution, as obtained by NMR and restrained molecular dynamics
    • Toiron C., Gonzalez C., Bruix M., Rico M. Three-dimensional structure of the complexes of ribonuclease A with 2′,5′-CpA and 3′,5′-d(CpA) in aqueous solution, as obtained by NMR and restrained molecular dynamics. Protein Sci. 5:1996;1633-1647.
    • (1996) Protein Sci. , vol.5 , pp. 1633-1647
    • Toiron, C.1    Gonzalez, C.2    Bruix, M.3    Rico, M.4
  • 21
    • 0030602895 scopus 로고    scopus 로고
    • X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 Å resolution
    • Mosimann S.C., Newton D.L., Youle R.J., James M.N. X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 Å resolution. J. Mol. Biol. 260:1996;540-552.
    • (1996) J. Mol. Biol. , vol.260 , pp. 540-552
    • Mosimann, S.C.1    Newton, D.L.2    Youle, R.J.3    James, M.N.4
  • 23
    • 0034725562 scopus 로고    scopus 로고
    • Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 Å resolution
    • Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T., Tada H., et al. Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 Å resolution. J. Mol. Biol. 300:2000;1297-1307.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1297-1307
    • Mallorqui-Fernandez, G.1    Pous, J.2    Peracaula, R.3    Aymami, J.4    Maeda, T.5    Tada, H.6
  • 24
    • 0033534398 scopus 로고    scopus 로고
    • The three-dimensional structure of human RNase 4, unliganded and complexed with d(Up), reveals the basis for its uridine selectivity
    • Terzyan S.S., Peracaula R., de Llorens R., Tsushima Y., Yamada H., Seno M., et al. The three-dimensional structure of human RNase 4, unliganded and complexed with d(Up), reveals the basis for its uridine selectivity. J. Mol. Biol. 285:1999;205-214.
    • (1999) J. Mol. Biol. , vol.285 , pp. 205-214
    • Terzyan, S.S.1    Peracaula, R.2    De Llorens, R.3    Tsushima, Y.4    Yamada, H.5    Seno, M.6
  • 25
    • 0028262928 scopus 로고
    • Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease
    • Acharya K.R., Shapiro R., Allen S.C., Riordan J.F., Vallee B.L. Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease. Proc. Natl Acad. Sci. USA. 91:1994;2915-2919.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2915-2919
    • Acharya, K.R.1    Shapiro, R.2    Allen, S.C.3    Riordan, J.F.4    Vallee, B.L.5
  • 26
    • 0030864496 scopus 로고    scopus 로고
    • Molecular recognition of human angiogenin by placental ribonuclease inhibitor - An X-ray crystallographic study at 2.0 Å resolution
    • Papageorgiou A.C., Shapiro R., Acharya K.R. Molecular recognition of human angiogenin by placental ribonuclease inhibitor - an X-ray crystallographic study at 2.0 Å resolution. EMBO J. 16:1997;5162-5177.
    • (1997) EMBO J. , vol.16 , pp. 5162-5177
    • Papageorgiou, A.C.1    Shapiro, R.2    Acharya, K.R.3
  • 27
    • 0028266432 scopus 로고
    • Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity
    • Mosimann S.C., Ardelt W., James M.N. Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity. J. Mol. Biol. 236:1994;1141-1153.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1141-1153
    • Mosimann, S.C.1    Ardelt, W.2    James, M.N.3
  • 28
    • 0032538276 scopus 로고    scopus 로고
    • The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeiana (bullfrog)
    • Chang C.F., Chen C., Chen Y.C., Hom K., Huang R.F., Huang T.H. The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeiana (bullfrog). J. Mol. Biol. 283:1998;231-244.
    • (1998) J. Mol. Biol. , vol.283 , pp. 231-244
    • Chang, C.F.1    Chen, C.2    Chen, Y.C.3    Hom, K.4    Huang, R.F.5    Huang, T.H.6
  • 29
    • 0034743773 scopus 로고    scopus 로고
    • 15N resonance assignments and secondary structure of the cytotoxic protein RNase 4 from bullfrog Rana catesbeiana oocytes
    • 15N resonance assignments and secondary structure of the cytotoxic protein RNase 4 from bullfrog Rana catesbeiana oocytes. J. Biomol. NMR. 20:2001;93-94.
    • (2001) J. Biomol. NMR , vol.20 , pp. 93-94
    • Hsu, C.H.1    Liao, Y.D.2    Wu, S.H.3    Chen, C.4
  • 30
    • 0030037085 scopus 로고    scopus 로고
    • Contribution of a tyrosine side chain to ribonuclease A catalysis and stability
    • Eberhardt E.S., Wittmayer P.K., Templer B.M., Raines R.T. Contribution of a tyrosine side chain to ribonuclease A catalysis and stability. Protein Sci. 5:1996;1697-1703.
    • (1996) Protein Sci. , vol.5 , pp. 1697-1703
    • Eberhardt, E.S.1    Wittmayer, P.K.2    Templer, B.M.3    Raines, R.T.4
  • 31
    • 0034746296 scopus 로고    scopus 로고
    • 13C resonance assignments and secondary structure determination of the RC-RNase 2 from oocytes of bullfrog Rana catesbeiana
    • 13C resonance assignments and secondary structure determination of the RC-RNase 2 from oocytes of bullfrog Rana catesbeiana. J. Biomol. NMR. 19:2001;87-88.
    • (2001) J. Biomol. NMR , vol.19 , pp. 87-88
    • Hsu, C.H.1    Chen, L.W.2    Liao, Y.D.3    Wu, S.H.4    Chen, C.5
  • 32
    • 0034742694 scopus 로고    scopus 로고
    • 13C resonance assignments and secondary structure of the liver ribonuclease from bullfrog Rana catesbeiana
    • 13C resonance assignments and secondary structure of the liver ribonuclease from bullfrog Rana catesbeiana. J. Biomol. NMR. 20:2001;189-190.
    • (2001) J. Biomol. NMR , vol.20 , pp. 189-190
    • Su, N.Y.1    Liao, Y.D.2    Chang, C.F.3    Wang, I.4    Chen, C.5
  • 33
    • 0014945686 scopus 로고
    • Absolute stereochemistry of the second step of ribonuclease action
    • Usher D.A., Richardson D.I. Jr, Eckstein F. Absolute stereochemistry of the second step of ribonuclease action. Nature. 228:1970;663-665.
    • (1970) Nature , vol.228 , pp. 663-665
    • Usher, D.A.1    Richardson D.I., Jr.2    Eckstein, F.3
  • 34
    • 0015252687 scopus 로고
    • Geometry of the first step in the reaction of ribonuclease-A (in-line geometry-uridine2′,3′-cyclic thiophosphate-31P NMR)
    • Usher D.A., Erenrich E.S., Eckstein F. Geometry of the first step in the reaction of ribonuclease-A (in-line geometry-uridine2′,3′-cyclic thiophosphate-31P NMR). Proc. Natl Acad. Sci. USA. 69:1972;115-118.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 115-118
    • Usher, D.A.1    Erenrich, E.S.2    Eckstein, F.3
  • 36
    • 0028806062 scopus 로고
    • Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites
    • Nogues M.V., Vilanova M., Cuchillo C.M. Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. Biochim. Biophys. Acta. 1253:1995;16-24.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 16-24
    • Nogues, M.V.1    Vilanova, M.2    Cuchillo, C.M.3
  • 37
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines R.T. Ribonuclease A. Chem. Rev. 98:1998;1045-1066.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 38
    • 0020772531 scopus 로고
    • Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transition-state analog
    • Wlodawer A., Miller M., Sjolin L. Active site of RNase: neutron diffraction study of a complex with uridine vanadate, a transition-state analog. Proc. Natl Acad. Sci. USA. 80:1983;3628-3631.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 3628-3631
    • Wlodawer, A.1    Miller, M.2    Sjolin, L.3
  • 41
    • 0028198937 scopus 로고
    • Yolk granules are the major compartment for bullfrog (Rana catesbeiana) oocyte-specific ribonuclease
    • Liao Y.D., Wang J.J. Yolk granules are the major compartment for bullfrog (Rana catesbeiana) oocyte-specific ribonuclease. Eur. J. Biochem. 222:1994;215-220.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 215-220
    • Liao, Y.D.1    Wang, J.J.2
  • 42
    • 0028843021 scopus 로고
    • Determination of base specificity of multiple ribonucleases from crude samples
    • Liao Y.D. Determination of base specificity of multiple ribonucleases from crude samples. Mol. Biol. Rep. 20:1994;149-154.
    • (1994) Mol. Biol. Rep. , vol.20 , pp. 149-154
    • Liao, Y.D.1
  • 43
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:2000;252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 44
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay L.E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog. Biophys. Mol. Biol. 63:1995;277-299.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 45
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 46
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c
    • Hyberts S.G., Marki W., Wagner G. Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c. Eur. J. Biochem. 164:1987;625-635.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Marki, W.2    Wagner, G.3
  • 47
  • 48
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;29-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 49
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 50
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 51
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 Å
    • Wlodawer A., Svensson L.A., Sjolin L., Gilliland G.L. Structure of phosphate-free ribonuclease A refined at 1.26 Å Biochemistry. 27:1988;2705-2717.
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjolin, L.3    Gilliland, G.L.4


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