메뉴 건너뛰기




Volumn 23, Issue 20, 2004, Pages 3929-3938

Structural basis for recognition of 2′,5′-linked oligoadenylates by human ribonuclease L

Author keywords

2 5A system; Ankyrin repeat; Crystal structure; Drug design; Interferon

Indexed keywords

2',5' OLIGOADENYLIC ACID; ANKYRIN; INTERFERON; NUCLEIC ACID; RIBONUCLEASE; RIBONUCLEASE L; RNA;

EID: 8144225873     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600420     Document Type: Article
Times cited : (83)

References (51)
  • 3
    • 0023194764 scopus 로고
    • Four different forms of interferon-treated 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells
    • Chebath J, Benech P, Hovanessian A, Galabru J, Revel M (1987) Four different forms of interferon-treated 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells. J Biol Chem 262: 3852-3857
    • (1987) J Biol Chem , vol.262 , pp. 3852-3857
    • Chebath, J.1    Benech, P.2    Hovanessian, A.3    Galabru, J.4    Revel, M.5
  • 4
    • 0029989326 scopus 로고    scopus 로고
    • Stoichiometry of 2′,5′-oligoadenylate-induced dimerization of ribonuclease L
    • Cole JL, Carroll SS, Kuo LC (1996) Stoichiometry of 2′,5′- oligoadenylate-induced dimerization of ribonuclease L. J Biol Chem 271: 3979-3981
    • (1996) J Biol Chem , vol.271 , pp. 3979-3981
    • Cole, J.L.1    Carroll, S.S.2    Kuo, L.C.3
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative computational project, number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 6
    • 0032979274 scopus 로고    scopus 로고
    • Full activation of RNase L in animal cells requires binding of 2-5A within ankyrin repeats 6 to 9 of this interferon-inducible enzyme
    • Diaz-Guerra M, Rivas C, Esteban M (1999) Full activation of RNase L in animal cells requires binding of 2-5A within ankyrin repeats 6 to 9 of this interferon-inducible enzyme. J Interferon Cytokine Res 19: 113-119
    • (1999) J Interferon Cytokine Res , vol.19 , pp. 113-119
    • Diaz-Guerra, M.1    Rivas, C.2    Esteban, M.3
  • 7
    • 0028909072 scopus 로고
    • 2-5A-dependent RNase molecules dimerize during activation by 2-5A
    • Dong B, Silverman RH (1995) 2-5A-dependent RNase molecules dimerize during activation by 2-5A. J Biol Chem 270: 4133-4137
    • (1995) J Biol Chem , vol.270 , pp. 4133-4137
    • Dong, B.1    Silverman, R.H.2
  • 8
    • 0030799121 scopus 로고    scopus 로고
    • A bipartite model of 2-5A-dependent RNase L
    • Dong B, Silverman RH (1997) A bipartite model of 2-5A-dependent RNase L. J Biol Chem 272: 22236-22242
    • (1997) J Biol Chem , vol.272 , pp. 22236-22242
    • Dong, B.1    Silverman, R.H.2
  • 10
    • 0020490460 scopus 로고
    • Structural requirements of (2′-5′) oligoadenylate for protein synthesis inhibition in human fibroblasts
    • Drocourt JL, Dieffenbach CW, Ts'o PO, Justesen J, Thang MN (1982) Structural requirements of (2′-5′) oligoadenylate for protein synthesis inhibition in human fibroblasts. Nucleic Acids Res 10: 2163-2174
    • (1982) Nucleic Acids Res , vol.10 , pp. 2163-2174
    • Drocourt, J.L.1    Dieffenbach, C.W.2    Ts'o, P.O.3    Justesen, J.4    Thang, M.N.5
  • 11
    • 0019794540 scopus 로고
    • Interferon action: RNA cleavage pattern of a (2′-5′) oligoadenylate-dependent endonuclease
    • Floyd-Smith G, Slattery E, Lengyel P (1981) Interferon action: RNA cleavage pattern of a (2′-5′)oligoadenylate-dependent endonuclease. Science 212: 1030-1032
    • (1981) Science , vol.212 , pp. 1030-1032
    • Floyd-Smith, G.1    Slattery, E.2    Lengyel, P.3
  • 12
    • 0344413485 scopus 로고    scopus 로고
    • Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′- oligoadenylate synthetase
    • Hartmann R, Justesen J, Sarker SN, Sen GS, Yee VC (2003) Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′-oligoadenylate synthetase. Mol Cell 19: 1173-1185
    • (2003) Mol Cell , vol.19 , pp. 1173-1185
    • Hartmann, R.1    Justesen, J.2    Sarker, S.N.3    Sen, G.S.4    Yee, V.C.5
  • 13
    • 0027270867 scopus 로고
    • A dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon
    • Hassel BA, Zhou A, Sotomayor C, Maran A, Silverman RH (1993) A dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon. EMBO J 12: 3297-3304
    • (1993) EMBO J , vol.12 , pp. 3297-3304
    • Hassel, B.A.1    Zhou, A.2    Sotomayor, C.3    Maran, A.4    Silverman, R.H.5
  • 15
    • 0017372188 scopus 로고
    • Synthesis of low molecular weight inhibitor of protein synthesis with enzyme from interferon-treated cells
    • Hovanessian A, Brown RE, Kerr IM (1977) Synthesis of low molecular weight inhibitor of protein synthesis with enzyme from interferon-treated cells. Nature 268: 537-539
    • (1977) Nature , vol.268 , pp. 537-539
    • Hovanessian, A.1    Brown, R.E.2    Kerr, I.M.3
  • 16
    • 0021981511 scopus 로고
    • Respective role of each of the purine N-6 amino groups of 5′-O-triphosphoryladenylyl(2′-5′)adenylyl(2′-5′) adenosine in binding to activation of RNase L
    • Imai J, Lesiak K, Torrence PF (1985) Respective role of each of the purine N-6 amino groups of 5′-O-triphosphoryladenylyl(2′-5′) adenylyl(2′-5′)adenosine in binding to activation of RNase L. J Biol Chem 260: 1390-1393
    • (1985) J Biol Chem , vol.260 , pp. 1390-1393
    • Imai, J.1    Lesiak, K.2    Torrence, P.F.3
  • 17
    • 84988072575 scopus 로고
    • Abbreviations and symbols for the description of conformations of polynucleotide chains
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature (1983) Abbreviations and symbols for the description of conformations of polynucleotide chains. Eur J Biochem 131: 9-15
    • (1983) Eur J Biochem , vol.131 , pp. 9-15
  • 18
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs MD, Harrison SC (1998) Structure of an IκBα/NF- κB complex. Cell 95: 749-758
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 19
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • Kawabata T (2003) MATRAS: a program for protein 3D structure comparison. Nucleic Acids Res 31: 3367-3369
    • (2003) Nucleic Acids Res , vol.31 , pp. 3367-3369
    • Kawabata, T.1
  • 20
    • 0013683658 scopus 로고
    • pppA2′p5′A2′p5′A: An inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells
    • Kerr IM, Brown RE (1978) pppA2′p5′A2′p5′A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells. Proc Natl Acad Sci USA 75: 256-260
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 256-260
    • Kerr, I.M.1    Brown, R.E.2
  • 21
    • 0001357528 scopus 로고
    • Uridine analogs of 2′,5′-oligoadenylates: On the biological role of the middle base of 2-5A trimer
    • Kitade Y, Alster DK, Pabuccuoglu A, Torrence PF (1991a) Uridine analogs of 2′,5′-oligoadenylates: on the biological role of the middle base of 2-5A trimer. Bioorg Chem 19: 283-299
    • (1991) Bioorg Chem , vol.19 , pp. 283-299
    • Kitade, Y.1    Alster, D.K.2    Pabuccuoglu, A.3    Torrence, P.F.4
  • 22
  • 24
    • 0034696057 scopus 로고    scopus 로고
    • 2-Methyladenosine-substituted 2′,5′-oligoadenylates: Conformations, 2-5A binding and catalytic activities with human ribonuclease L
    • Kitade Y, Wakana M, Tsuboi T, Yatome C, Bayly SF, Player MR, Torrence PF (2000) 2-Methyladenosine-substituted 2′,5′-oligoadenylates: conformations, 2-5A binding and catalytic activities with human ribonuclease L. Bioorg Med Chem Lett 10: 329-331
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 329-331
    • Kitade, Y.1    Wakana, M.2    Tsuboi, T.3    Yatome, C.4    Bayly, S.F.5    Player, M.R.6    Torrence, P.F.7
  • 26
    • 0347093301 scopus 로고    scopus 로고
    • The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator, and the tumor suppressors Rb and p53
    • Krzywda S, Brzozowski AM, Higashitsuji H, Fujita J, Welchman R, Dawson S, Mayer RJ, Wilkinson AJ (2004) The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator, and the tumor suppressors Rb and p53. J Biol Chem 279: 1541-1545
    • (2004) J Biol Chem , vol.279 , pp. 1541-1545
    • Krzywda, S.1    Brzozowski, A.M.2    Higashitsuji, H.3    Fujita, J.4    Welchman, R.5    Dawson, S.6    Mayer, R.J.7    Wilkinson, A.J.8
  • 27
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin V, Wilson KS (1993) Automated refinement of protein models. Acta Crystallogr D 49: 129-147
    • (1993) Acta Crystallogr D , vol.49 , pp. 129-147
    • Lamzin, V.1    Wilson, K.S.2
  • 28
  • 29
    • 0021100299 scopus 로고
    • Biological activities of phosphodiester linkage isomers of 2-5A
    • Lesiak K, Imai J, Floyd-Smith G, Torrence PF (1983) Biological activities of phosphodiester linkage isomers of 2-5A. J Biol Chem 258: 13082-13088
    • (1983) J Biol Chem , vol.258 , pp. 13082-13088
    • Lesiak, K.1    Imai, J.2    Floyd-Smith, G.3    Torrence, P.F.4
  • 30
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux SE, John KM, Bennett V (1990) Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 344: 36-42
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 31
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee DE (1999) XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156-165
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 32
    • 0028057108 scopus 로고
    • RasterSD version 2.0: A program for photorealistic molecular graphics
    • Merritt EA, Murphy EP (1994) RasterSD version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr D 50: 869-873
    • (1994) Acta Crystallogr D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, E.P.2
  • 33
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • Michaely P, Tomchick DR, Machius M, Anderson RGW (2002) Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J 21: 6387-6396
    • (2002) EMBO J , vol.21 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.W.4
  • 34
    • 0035890072 scopus 로고    scopus 로고
    • Crystal structure of the ankyrin repeat domain of Bcl-3: A unique member of the IκB protein family
    • Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Muller CW (2001) Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IκB protein family. EMBO J 20: 6180-6190
    • (2001) EMBO J , vol.20 , pp. 6180-6190
    • Michel, F.1    Soler-Lopez, M.2    Petosa, C.3    Cramer, P.4    Siebenlist, U.5    Muller, C.W.6
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 3042805459 scopus 로고    scopus 로고
    • Contribution of Tyr712 and Phe716 to the activity of human RNase L
    • Nakanishi M, Yoshimura A, Ishida N, Ueno Y, Kitade Y (2004) Contribution of Tyr712 and Phe716 to the activity of human RNase L. Eur J Biochem 271: 2737-2744
    • (2004) Eur J Biochem , vol.271 , pp. 2737-2744
    • Nakanishi, M.1    Yoshimura, A.2    Ishida, N.3    Ueno, Y.4    Kitade, Y.5
  • 37
    • 84920325457 scopus 로고
    • AMoRe: An automated program for molecular replacement
    • Navaza J (1994) AMoRe: an automated program for molecular replacement. Acta Crystallogr A 50: 157-163
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 38
    • 0026365944 scopus 로고
    • The antiviral potentials of Mx proteins
    • Pavlovic J, Staeheli P (1991) The antiviral potentials of Mx proteins. J Interferon Res 11: 215-219
    • (1991) J Interferon Res , vol.11 , pp. 215-219
    • Pavlovic, J.1    Staeheli, P.2
  • 39
    • 0032079356 scopus 로고    scopus 로고
    • The 2-5A system: Modulation of viral and cellular processes through acceleration of RNA degradation
    • Player MR, Torrence PF (1998) The 2-5A system: modulation of viral and cellular processes through acceleration of RNA degradation. Pharmacol Ther 78: 55-113
    • (1998) Pharmacol Ther , vol.78 , pp. 55-113
    • Player, M.R.1    Torrence, P.F.2
  • 41
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: A diversity of interactions on a common structural framework
    • Sedwick SG, Smerdon SJ (1999) The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem Sci 24: 311-316
    • (1999) Trends Biochem Sci , vol.24 , pp. 311-316
    • Sedwick, S.G.1    Smerdon, S.J.2
  • 42
    • 0034769960 scopus 로고    scopus 로고
    • Viruses and interferons
    • Sen GC (2001) Viruses and interferons. Annu Rev Microbiol 55: 255-281
    • (2001) Annu Rev Microbiol , vol.55 , pp. 255-281
    • Sen, G.C.1
  • 44
    • 0024296206 scopus 로고
    • Only one 3′-hydroxyl group of ppp5′A2′p5′ A2′p5′A (2-5A) is required for activation of the 2-5A-dependent endonuclease
    • Torrence PF, Brozda D, Alster D, Charubala R, Pfleiderer W (1988) Only one 3′-hydroxyl group of ppp5′A2′p5′A2′p5′A (2-5A) is required for activation of the 2-5A-dependent endonuclease. J Biol Chem 263: 1131-1139
    • (1988) J Biol Chem , vol.263 , pp. 1131-1139
    • Torrence, P.F.1    Brozda, D.2    Alster, D.3    Charubala, R.4    Pfleiderer, W.5
  • 45
    • 0021269173 scopus 로고
    • Oligonucleotide structural parameters that influence binding of 5′-O-triphosphoryladenylyl(2′-5′)adenylyl(2′-5′) adenosine to the 5′-O-triphosphoryladenylyl(2′-5′) adenylyl(2′-5′)adenosine-dependent endoribonuclease: Chain length, phosphorylation state, and heterocyclic base
    • Torrence PF, Imai J, Lesiak K, Jamoulle J-C, Sawai H (1984) Oligonucleotide structural parameters that influence binding of 5′-O-triphosphoryladenylyl(2′-5′)adenylyl(2′-5′) adenosine to the 5′-O-triphosphoryladenylyl(2′-5′) adenylyl(2′-5′)adenosine-dependent endoribonuclease: chain length, phosphorylation state, and heterocyclic base. J Med Chem 27: 726-733
    • (1984) J Med Chem , vol.27 , pp. 726-733
    • Torrence, P.F.1    Imai, J.2    Lesiak, K.3    Jamoulle, J.-C.4    Sawai, H.5
  • 46
    • 0028313602 scopus 로고
    • Development of 2′,5′-oligonucleotides as potential therapeutic agents
    • Torrence PF, Xiao W, Li G, Khamnei S (1994) Development of 2′,5′-oligonucleotides as potential therapeutic agents. Curr Med Chem 1: 176-191
    • (1994) Curr Med Chem , vol.1 , pp. 176-191
    • Torrence, P.F.1    Xiao, W.2    Li, G.3    Khamnei, S.4
  • 47
    • 0028797781 scopus 로고
    • The role of the dsRNA-activated kinase, PKR, in signal transduction
    • Williams BRG (1995) The role of the dsRNA-activated kinase, PKR, in signal transduction. Semin Virol 6: 191-202
    • (1995) Semin Virol , vol.6 , pp. 191-202
    • Williams, B.R.G.1
  • 50
    • 0036775461 scopus 로고    scopus 로고
    • Comparative study on the biological properties of 2′,5′- oligoadenylate derivatives with purified human RNase L expressed in E. coli
    • Yoshimura A, Nakanishi M, Yatome C, Kitade Y (2002) Comparative study on the biological properties of 2′,5′-oligoadenylate derivatives with purified human RNase L expressed in E. coli. J Biochem 132: 643-648
    • (2002) J Biochem , vol.132 , pp. 643-648
    • Yoshimura, A.1    Nakanishi, M.2    Yatome, C.3    Kitade, Y.4
  • 51
    • 0027510449 scopus 로고
    • Expression cloning of 2-5A-dependent RNAase: A uniquely regulated mediator of interferon action
    • Zhou A, Hassel BA, Silverman RH (1993) Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action. Cell 72: 753-765
    • (1993) Cell , vol.72 , pp. 753-765
    • Zhou, A.1    Hassel, B.A.2    Silverman, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.