메뉴 건너뛰기




Volumn 95, Issue 7, 1998, Pages 963-974

Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; SINGLE STRANDED DNA;

EID: 0032431057     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81720-1     Document Type: Article
Times cited : (232)

References (54)
  • 1
    • 0025731583 scopus 로고
    • Structure and function of telomeres
    • Blackburn, E.H. (1991). Structure and function of telomeres. Nature 350, 569-573.
    • (1991) Nature , vol.350 , pp. 569-573
    • Blackburn, E.H.1
  • 2
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., Pfuetzner, R.A., Edwards, A.M., and Frappier, L. (1997). Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385, 176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 7
    • 0032128419 scopus 로고    scopus 로고
    • Miscellaneous algorithms for density modification
    • Cowtan, K., and Main, P. (1998). Miscellaneous algorithms for density modification. Acta Crystallogr. D 54, 487-493.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 487-493
    • Cowtan, K.1    Main, P.2
  • 8
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology:A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D.A. (1996). Cation-pi interactions in chemistry and biology:a new view of benzene, Phe, Tyr, and Trp. Science 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 9
    • 0026091685 scopus 로고
    • Molecular cloning of telomere-binding protein genes from Stylonychia mytilis
    • Fang, G.W., and Cech, T.R. (1991). Molecular cloning of telomere-binding protein genes from Stylonychia mytilis. Nucleic Acids Res. 19, 5515-5518.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5515-5518
    • Fang, G.W.1    Cech, T.R.2
  • 10
    • 0027220845 scopus 로고
    • The beta subunit of Oxytricha telomere-binding protein promotes G-quartet formation by telomeric DNA
    • Fang, G., and Cech, T.R. (1993a). The beta subunit of Oxytricha telomere-binding protein promotes G-quartet formation by telomeric DNA. Cell 74, 875-885.
    • (1993) Cell , vol.74 , pp. 875-885
    • Fang, G.1    Cech, T.R.2
  • 11
    • 0027163938 scopus 로고
    • Oxytricha telomere-binding protein: DNA-dependent dimerization of the alpha and beta subunits
    • Fang, G., and Cech, T.R. (1993b). Oxytricha telomere-binding protein: DNA-dependent dimerization of the alpha and beta subunits. Proc. Natl. Acad. Sci. USA 90, 6056-6060.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6056-6060
    • Fang, G.1    Cech, T.R.2
  • 12
    • 0027168268 scopus 로고
    • Oxytricha telomere-binding protein: Separable DNA-binding and dimerization domains of the alpha-subunit
    • Fang, G., Gray, J.T., and Cech, T.R. (1993). Oxytricha telomere-binding protein: separable DNA-binding and dimerization domains of the alpha-subunit. Genes Dev. 7, 870-882.
    • (1993) Genes Dev. , vol.7 , pp. 870-882
    • Fang, G.1    Gray, J.T.2    Cech, T.R.3
  • 15
    • 0023037564 scopus 로고
    • Telomere proteins: Specific recognition and protection of the natural termini of Oxytricha macronuclear DNA
    • Gottschling, D.E., and Zakian, V.A. (1986). Telomere proteins: specific recognition and protection of the natural termini of Oxytricha macronuclear DNA. Cell 47, 195-205.
    • (1986) Cell , vol.47 , pp. 195-205
    • Gottschling, D.E.1    Zakian, V.A.2
  • 16
    • 0025984268 scopus 로고
    • Cloning and expression of genes for the Oxytricha telomere-binding protein: Specific subunit interactions in the telomeric complex
    • Gray, J.T., Celander, D.W., Price, C.M., and Cech, T.R. (1991). Cloning and expression of genes for the Oxytricha telomere-binding protein: specific subunit interactions in the telomeric complex. Cell 67, 807-814.
    • (1991) Cell , vol.67 , pp. 807-814
    • Gray, J.T.1    Celander, D.W.2    Price, C.M.3    Cech, T.R.4
  • 17
    • 0022402513 scopus 로고
    • Identification of a specific telomere terminal transferase activity in Tetrahymena extracts
    • Greider, C.W., and Blackburn, E.H. (1985). Identification of a specific telomere terminal transferase activity in Tetrahymena extracts. Cell 43, 405-413.
    • (1985) Cell , vol.43 , pp. 405-413
    • Greider, C.W.1    Blackburn, E.H.2
  • 18
    • 0015519015 scopus 로고
    • Oligonucleotide conformations. Optical studies on GpU analogues with modified-uridine residues
    • Guschlbauer, W., Fric, I., and Holy, A. (1972). Oligonucleotide conformations. Optical studies on GpU analogues with modified-uridine residues. Eur. J. Biochem. 31, 1-13.
    • (1972) Eur. J. Biochem. , vol.31 , pp. 1-13
    • Guschlbauer, W.1    Fric, I.2    Holy, A.3
  • 19
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley, C.B., Futcher, A.B., and Greider, C.W. (1990). Telomeres shorten during ageing of human fibroblasts. Nature 345, 458-460.
    • (1990) Nature , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, A.B.2    Greider, C.W.3
  • 20
    • 0024573115 scopus 로고
    • An overhanging 3́ terminus is a conserved feature of telomeres
    • Henderson, E.R., and Blackburn, E.H. (1989). An overhanging 3́ terminus is a conserved feature of telomeres. Mol. Cell. Biol. 9, 345-38.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 345-438
    • Henderson, E.R.1    Blackburn, E.H.2
  • 21
    • 0028323417 scopus 로고
    • Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromodeoxyuridine
    • Hicke, B.J., Willis, M.C., Koch, T.H., and Cech, T.R. (1994). Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromodeoxyuridine. Biochemistry 33, 3364-3373.
    • (1994) Biochemistry , vol.33 , pp. 3364-3373
    • Hicke, B.J.1    Willis, M.C.2    Koch, T.H.3    Cech, T.R.4
  • 22
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S., and Chothia, C. (1988). Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 24
    • 0019568388 scopus 로고
    • All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus
    • Klobutcher, L.A., Swanton, M.T., Donini, P., and Prescott, D.M. (1981). All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus. Proc. Natl. Acad. Sci. USA 78, 3015-3019.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3015-3019
    • Klobutcher, L.A.1    Swanton, M.T.2    Donini, P.3    Prescott, D.M.4
  • 26
    • 0030447657 scopus 로고    scopus 로고
    • The Saccharomyces CDC13 protein is a single-strand TG1-3 telomeric DMA-binding protein in vitro that affects telomere behavior in vivo
    • Lin, J.J., and Zakian, V.A. (1996). The Saccharomyces CDC13 protein is a single-strand TG1-3 telomeric DMA-binding protein in vitro that affects telomere behavior in vivo. Proc. Natl. Acad. Sci. USA 93, 13760-13765.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13760-13765
    • Lin, J.J.1    Zakian, V.A.2
  • 27
    • 0029763191 scopus 로고    scopus 로고
    • Purification of telomerase from Euplotes aediculatus: Requirement of a primer 3′ overhang
    • Lingner, J., and Cech, T.R. (1996). Purification of telomerase from Euplotes aediculatus: requirement of a primer 3′ overhang. Proc. Natl. Acad. Sci. USA 93, 10712-10717.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10712-10717
    • Lingner, J.1    Cech, T.R.2
  • 28
    • 0024973811 scopus 로고
    • A mutant with a defect in telomere elongation leads to senescence in yeast
    • Lundblad, V., and Szostak, J.W. (1989). A mutant with a defect in telomere elongation leads to senescence in yeast. Cell 57, 633-643.
    • (1989) Cell , vol.57 , pp. 633-643
    • Lundblad, V.1    Szostak, J.W.2
  • 29
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (elF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., Gingras, A.C., Sonenberg, N., and Burley, S.K. (1997). Cocrystal structure of the messenger RNA 5′ cap-binding protein (elF4E) bound to 7-methyl-GDP. Cell 89, 951-961.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 30
    • 0001294157 scopus 로고
    • The stability of broken ends of chromosomes in Zea mays
    • McClintock, B. (1941). The stability of broken ends of chromosomes in Zea mays. Genetics 26, 234-282.
    • (1941) Genetics , vol.26 , pp. 234-282
    • McClintock, B.1
  • 31
    • 0030982721 scopus 로고    scopus 로고
    • The terminal DNA structure of mammalian chromosomes
    • McElligott, R., and Wellinger, R.J. (1997). The terminal DNA structure of mammalian chromosomes. EMBO J. 16, 3705-3714.
    • (1997) EMBO J. , vol.16 , pp. 3705-3714
    • McElligott, R.1    Wellinger, R.J.2
  • 32
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. (1993). OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 33
    • 0029845892 scopus 로고    scopus 로고
    • Cdc13p: A single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance
    • Nugent, C.I., Hughes, T.R., Lue, N.F., and Lundblad, V. (1996). Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance. Science 274, 249-252.
    • (1996) Science , vol.274 , pp. 249-252
    • Nugent, C.I.1    Hughes, T.R.2    Lue, N.F.3    Lundblad, V.4
  • 34
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. Daresbury UK: Daresbury Laboratory
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering, W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Daresbury UK: Daresbury Laboratory).
    • (1991) Isomorphous Replacement and Anomalous Scattering
    • Otwinowski, Z.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collectin in oscillation mode
    • Otwinowski, Z., and Minor, W. (1996). Processing of x-ray diffraction data collectin in oscillation mode. Methods Enzmol. 276, 307-326.
    • (1996) Methods Enzmol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.H., and Nagai, K. (1994). Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 37
    • 0023433713 scopus 로고
    • Telomeric DNA-protein interactions of Oxytricha macronuclear DNA
    • Price, C.M., and Cech, T.R. (1987). Telomeric DNA-protein interactions of Oxytricha macronuclear DNA. Genes Dev. 1, 783-793.
    • (1987) Genes Dev. , vol.1 , pp. 783-793
    • Price, C.M.1    Cech, T.R.2
  • 38
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA
    • Price, S.R., Evans, P.R., and Nagai, K. (1998). Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA. Nature 394, 645-650.
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evans, P.R.2    Nagai, K.3
  • 39
    • 0025079955 scopus 로고
    • Effect of monovalent cation-induced telomeric DNA structure on the binding of Oxytricha telomeric protein
    • Raghuraman, M.K., and Cech, T.R. (1990). Effect of monovalent cation-induced telomeric DNA structure on the binding of Oxytricha telomeric protein. Nucleic Acids Res. 18, 4543-4552.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4543-4552
    • Raghuraman, M.K.1    Cech, T.R.2
  • 40
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 41
    • 0024392753 scopus 로고
    • Structure of E. Coli glutaminyl-tRNA synthetase complexed with tRNA(GIn) and ATP at 2.8 å resolution
    • Rould, M.A., Perona, J.J., Soll, D., and Steitz, T.A. (1989). Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(GIn) and ATP at 2.8 Å resolution. Science 246, 1135-1142.
    • (1989) Science , vol.246 , pp. 1135-1142
    • Rould, M.A.1    Perona, J.J.2    Soll, D.3    Steitz, T.A.4
  • 42
    • 0026429275 scopus 로고
    • Class II aminoacyl transfer RNA synthetases: Crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)
    • Ruff, M., Krishnaswamy, S., Boeglin, M., Poterszman, A., Mitschler, A., Podjarny, A., Rees, B., Thierry, J.C., and Moras, D. (1991). Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252, 1682-1689.
    • (1991) Science , vol.252 , pp. 1682-1689
    • Ruff, M.1    Krishnaswamy, S.2    Boeglin, M.3    Poterszman, A.4    Mitschler, A.5    Podjarny, A.6    Rees, B.7    Thierry, J.C.8    Moras, D.9
  • 44
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Shamoo, Y., Friedman, A.M., Parsons, M.R., Konigsberg, W.H., and Steitz, T.A. (1995). Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature 376, 362-366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 45
    • 0030857774 scopus 로고    scopus 로고
    • Telomerase and telomere-binding proteins: Controlling the endgame
    • Shore, D. (1997). Telomerase and telomere-binding proteins: controlling the endgame. Trends Biochem. Sci. 22, 233-235.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 233-235
    • Shore, D.1
  • 46
    • 0015430524 scopus 로고
    • Flexibility and conformations of guanosine monophosphates by the overhauser effect
    • Son, T.D., Guschlbauer, W., and Gueron, M. (1972). Flexibility and conformations of guanosine monophosphates by the Overhauser effect. J. Am. Chem. Soc. 94, 7903-7911.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 7903-7911
    • Son, T.D.1    Guschlbauer, W.2    Gueron, M.3
  • 47
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S., and Record, M.T., Jr. (1994). Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record M.T., Jr.2
  • 48
    • 0024843757 scopus 로고
    • Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops
    • Sundquist, W.I., and Klug, A. (1989). Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops. Nature 342, 825-829.
    • (1989) Nature , vol.342 , pp. 825-829
    • Sundquist, W.I.1    Klug, A.2
  • 49
    • 0027976323 scopus 로고
    • Telomeric DNA sequence and structure following de novo telomere synthesis in Euplotes crassus
    • Vermeesch, J.R., and Price, C.M. (1994). Telomeric DNA sequence and structure following de novo telomere synthesis in Euplotes crassus. Mol. Cell. Biol. 14, 554-566.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 554-566
    • Vermeesch, J.R.1    Price, C.M.2
  • 50
    • 0030462146 scopus 로고    scopus 로고
    • Est1 has the properties of a single-stranded telomere end-binding protein
    • Virta-Pearlman, V., Morris, D.K., and Lundblad, V. (1996). Est1 has the properties of a single-stranded telomere end-binding protein. Genes Dev. 10, 3094-3104.
    • (1996) Genes Dev. , vol.10 , pp. 3094-3104
    • Virta-Pearlman, V.1    Morris, D.K.2    Lundblad, V.3
  • 51
    • 0027104087 scopus 로고
    • Euplotes crassus has genes encoding telomere-binding proteins and telomere-binding protein homologs
    • Wang, W., Skopp, R., Scofield, M., and Price, C. (1992). Euplotes crassus has genes encoding telomere-binding proteins and telomere-binding protein homologs. Nucleic Acids Res. 20, 6621-6629.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6621-6629
    • Wang, W.1    Skopp, R.2    Scofield, M.3    Price, C.4
  • 52
    • 0024787884 scopus 로고
    • Monovalent cation-induced structure of telomeric DNA: The G-quartet model
    • Williamson, J.R., Raghuraman, M.K., and Cech, T.R. (1989). Monovalent cation-induced structure of telomeric DNA: the G-quartet model. Cell 59, 871-880.
    • (1989) Cell , vol.59 , pp. 871-880
    • Williamson, J.R.1    Raghuraman, M.K.2    Cech, T.R.3
  • 53
    • 0025279059 scopus 로고
    • In vivo alteration of telomere sequences and senescence caused by mutated Tetrahymena telomerase RNAs
    • Yu, G.L., Bradley, J.D., Attardi, L.D., and Blackburn, E.H. (1990). In vivo alteration of telomere sequences and senescence caused by mutated Tetrahymena telomerase RNAs. Nature 344, 126-132.
    • (1990) Nature , vol.344 , pp. 126-132
    • Yu, G.L.1    Bradley, J.D.2    Attardi, L.D.3    Blackburn, E.H.4
  • 54
    • 0029563009 scopus 로고
    • Telomeres: Beginning to understand the end
    • Zakian, V.A. (1995). Telomeres: beginning to understand the end. Science 270, 1601-1607.
    • (1995) Science , vol.270 , pp. 1601-1607
    • Zakian, V.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.