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Volumn 21, Issue 1, 2013, Pages 121-132

Nonspecific recognition is achieved in pot1pc through the use of multiple binding modes

Author keywords

[No Author keywords available]

Indexed keywords

OLIGONUCLEOTIDE; OLIGOSACCHARIDE; PROTEIN DERIVATIVE; PROTEIN POT1PC; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84872134476     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.10.015     Document Type: Article
Times cited : (23)

References (45)
  • 2
    • 80052248612 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences
    • S.E. Altschuler, T.H. Dickey, and D.S. Wuttke Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences Biochemistry 50 2011 7503 7513
    • (2011) Biochemistry , vol.50 , pp. 7503-7513
    • Altschuler, S.E.1    Dickey, T.H.2    Wuttke, D.S.3
  • 3
    • 0037426333 scopus 로고    scopus 로고
    • Site-directed mutagenesis reveals the thermodynamic requirements for single-stranded DNA recognition by the telomere-binding protein Cdc13
    • DOI 10.1021/bi027047c
    • E.M. Anderson, W.A. Halsey, and D.S. Wuttke Site-directed mutagenesis reveals the thermodynamic requirements for single-stranded DNA recognition by the telomere-binding protein Cdc13 Biochemistry 42 2003 3751 3758 (Pubitemid 36402668)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3751-3758
    • Anderson, E.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 4
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • DOI 10.1126/science.1060036
    • P. Baumann, and T.R. Cech Pot1, the putative telomere end-binding protein in fission yeast and humans Science 292 2001 1171 1175 (Pubitemid 32440940)
    • (2001) Science , vol.292 , Issue.5519 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 7
    • 33747751221 scopus 로고    scopus 로고
    • Themes in ssDNA recognition by telomere-end protection proteins
    • DOI 10.1016/j.tibs.2006.07.004, PII S0968000406001952
    • J.E. Croy, and D.S. Wuttke Themes in ssDNA recognition by telomere-end protection proteins Trends Biochem. Sci. 31 2006 516 525 (Pubitemid 44279982)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.9 , pp. 516-525
    • Croy, J.E.1    Wuttke, D.S.2
  • 8
    • 33745906967 scopus 로고    scopus 로고
    • 1-389
    • DOI 10.1016/j.jmb.2006.06.002, PII S0022283606006930
    • J.E. Croy, E.R. Podell, and D.S. Wuttke A new model for Schizosaccharomyces pombe telomere recognition: the telomeric single-stranded DNA-binding activity of Pot11-389 J. Mol. Biol. 361 2006 80 93 (Pubitemid 44041454)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.1 , pp. 80-93
    • Croy, J.E.1    Podell, E.R.2    Wuttke, D.S.3
  • 9
    • 67651230533 scopus 로고    scopus 로고
    • Nonadditivity in the recognition of single-stranded DNA by the Schizosaccharomyces pombe protection of telomeres 1 DNA-binding domain, Pot1-DBD
    • J.E. Croy, S.E. Altschuler, N.E. Grimm, and D.S. Wuttke Nonadditivity in the recognition of single-stranded DNA by the Schizosaccharomyces pombe protection of telomeres 1 DNA-binding domain, Pot1-DBD Biochemistry 48 2009 6864 6875
    • (2009) Biochemistry , vol.48 , pp. 6864-6875
    • Croy, J.E.1    Altschuler, S.E.2    Grimm, N.E.3    Wuttke, D.S.4
  • 10
    • 84855343723 scopus 로고    scopus 로고
    • A syn-anti conformational difference allows SRSF2 to recognize guanines and cytosines equally well
    • G.M. Daubner, A. Cléry, S. Jayne, J. Stevenin, and F.H.-T. Allain A syn-anti conformational difference allows SRSF2 to recognize guanines and cytosines equally well EMBO J. 31 2012 162 174
    • (2012) EMBO J. , vol.31 , pp. 162-174
    • Daubner, G.M.1    Cléry, A.2    Jayne, S.3    Stevenin, J.4    Allain, F.H.-T.5
  • 11
    • 71149093724 scopus 로고    scopus 로고
    • How telomeres solve the end-protection problem
    • T. de Lange How telomeres solve the end-protection problem Science 326 2009 948 952
    • (2009) Science , vol.326 , pp. 948-952
    • De Lange, T.1
  • 12
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • DOI 10.1038/nature06065, PII NATURE06065
    • E.L. Denchi, and T. de Lange Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1 Nature 448 2007 1068 1071 (Pubitemid 47345583)
    • (2007) Nature , vol.448 , Issue.7157 , pp. 1068-1071
    • Denchi, E.L.1    De Lange, T.2
  • 13
    • 31044455231 scopus 로고    scopus 로고
    • Identification of the determinants for the specific recognition of single-strand telomeric DNA by Cdc13
    • DOI 10.1021/bi0512703
    • A.M. Eldridge, W.A. Halsey, and D.S. Wuttke Identification of the determinants for the specific recognition of single-strand telomeric DNA by Cdc13 Biochemistry 45 2006 871 879 (Pubitemid 43122251)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 871-879
    • Eldridge, A.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 15
    • 0034662244 scopus 로고    scopus 로고
    • Telomerase-dependent repeat divergence at the 3' ends of yeast telomeres
    • K. Förstemann, M. Höss, and J. Lingner Telomerase-dependent repeat divergence at the 3′ ends of yeast telomeres Nucleic Acids Res. 28 2000 2690 2694 (Pubitemid 30488012)
    • (2000) Nucleic Acids Research , vol.28 , Issue.14 , pp. 2690-2694
    • Forstemann, K.1    Hoss, M.2    Lingner, J.3
  • 16
    • 0025851273 scopus 로고
    • Structural aspects of protein-DNA recognition
    • P.S. Freemont, A.N. Lane, and M.R. Sanderson Structural aspects of protein-DNA recognition Biochem. J. 278 1991 1 23
    • (1991) Biochem. J. , vol.278 , pp. 1-23
    • Freemont, P.S.1    Lane, A.N.2    Sanderson, M.R.3
  • 17
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • WEB SERVER ISSUE
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 Web Server issue 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 18
    • 80053464451 scopus 로고    scopus 로고
    • Structural anatomy of telomere OB proteins
    • M.P. Horvath Structural anatomy of telomere OB proteins Crit. Rev. Biochem. Mol. Biol. 46 2011 409 435
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 409-435
    • Horvath, M.P.1
  • 19
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • DOI 10.1016/S0092-8674(00)81720-1
    • M.P. Horvath, V.L. Schweiker, J.M. Bevilacqua, J.A. Ruggles, and S.C. Schultz Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA Cell 95 1998 963 974 (Pubitemid 29019048)
    • (1998) Cell , vol.95 , Issue.7 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 20
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J.E. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 21
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • T.S. Krishna, X.P. Kong, S. Gary, P.M. Burgers, and J. Kuriyan Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA Cell 79 1994 1233 1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 22
    • 12844265975 scopus 로고    scopus 로고
    • Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
    • M. Lei, E.R. Podell, and T.R. Cech Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection Nat. Struct. Mol. Biol. 11 2004 1223 1229
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1223-1229
    • Lei, M.1    Podell, E.R.2    Cech, T.R.3
  • 24
    • 84855763327 scopus 로고    scopus 로고
    • Telomerase and telomere-associated proteins: Structural insights into mechanism and evolution
    • K.A. Lewis, and D.S. Wuttke Telomerase and telomere-associated proteins: structural insights into mechanism and evolution Structure 20 2012 28 39
    • (2012) Structure , vol.20 , pp. 28-39
    • Lewis, K.A.1    Wuttke, D.S.2
  • 25
    • 0042525860 scopus 로고    scopus 로고
    • DNA binding and cleavage by the periplasmic nuclease Vvn: A novel structure with a known active site
    • DOI 10.1093/emboj/cdg377
    • C.-L. Li, L.-I. Hor, Z.-F. Chang, L.-C. Tsai, W.-Z. Yang, and H.S. Yuan DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site EMBO J. 22 2003 4014 4025 (Pubitemid 36975727)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 4014-4025
    • Li, C.-L.1    Hor, L.-I.2    Chang, Z.-F.3    Tsai, L.-C.4    Yang, W.-Z.5    Yuan, H.S.6
  • 26
    • 79952460244 scopus 로고    scopus 로고
    • Alternate modes of cognate RNA recognition by human PUMILIO proteins
    • G. Lu, and T.M.T. Hall Alternate modes of cognate RNA recognition by human PUMILIO proteins Structure 19 2011 361 367
    • (2011) Structure , vol.19 , pp. 361-367
    • Lu, G.1    Hall, T.M.T.2
  • 27
    • 2442664066 scopus 로고    scopus 로고
    • Structural basis of single-stranded RNA recognition
    • A.C. Messias, and M. Sattler Structural basis of single-stranded RNA recognition Acc. Chem. Res. 37 2004 279 287
    • (2004) Acc. Chem. Res. , vol.37 , pp. 279-287
    • Messias, A.C.1    Sattler, M.2
  • 28
    • 0037023303 scopus 로고    scopus 로고
    • Conserved structure for single-stranded telomeric DNA recognition
    • DOI 10.1126/science.1068799
    • R.M. Mitton-Fry, E.M. Anderson, T.R. Hughes, V. Lundblad, and D.S. Wuttke Conserved structure for single-stranded telomeric DNA recognition Science 296 2002 145 147 (Pubitemid 34280074)
    • (2002) Science , vol.296 , Issue.5565 , pp. 145-147
    • Mitton-Fry, R.M.1    Anderson, E.M.2    Hughes, T.R.3    Lundblad, V.4    Wuttke, D.S.5
  • 29
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • DOI 10.1038/313762a0
    • D.L. Ollis, P. Brick, R. Hamlin, N.G. Xuong, and T.A. Steitz Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP Nature 313 1985 762 766 (Pubitemid 15130824)
    • (1985) Nature , vol.313 , Issue.6005 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode J.Charles W. Carter, Macromolecular Crystallography Part A 1997 Academic Press New York 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0033887437 scopus 로고    scopus 로고
    • Structure of the DNA binding domain of E. coli SSB bound to ssDNA
    • DOI 10.1038/77943
    • S. Raghunathan, A.G. Kozlov, T.M. Lohman, and G. Waksman Structure of the DNA binding domain of E. coli SSB bound to ssDNA Nat. Struct. Biol. 7 2000 648 652 (Pubitemid 30636675)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 648-652
    • Raghunathan, S.1    Kozlov, A.G.2    Lohman, T.M.3    Waksman, G.4
  • 32
    • 77955419733 scopus 로고    scopus 로고
    • The function of classical and alternative non-homologous end-joining pathways in the fusion of dysfunctional telomeres
    • R. Rai, H. Zheng, H. He, Y. Luo, A. Multani, P.B. Carpenter, and S. Chang The function of classical and alternative non-homologous end-joining pathways in the fusion of dysfunctional telomeres EMBO J. 29 2010 2598 2610
    • (2010) EMBO J. , vol.29 , pp. 2598-2610
    • Rai, R.1    Zheng, H.2    He, H.3    Luo, Y.4    Multani, A.5    Carpenter, P.B.6    Chang, S.7
  • 33
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • M.T. Record Jr., M.L. Lohman, and P. De Haseth Ion effects on ligand-nucleic acid interactions J. Mol. Biol. 107 1976 145 158
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, Jr.M.T.1    Lohman, M.L.2    De Haseth, P.3
  • 35
    • 0042035638 scopus 로고    scopus 로고
    • Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes
    • DOI 10.1093/emboj/cdg415
    • D.L. Theobald, and S.C. Schultz Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes EMBO J. 22 2003 4314 4324 (Pubitemid 37021758)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4314-4324
    • Theobald, D.L.1    Schultz, S.C.2
  • 36
    • 4644220875 scopus 로고    scopus 로고
    • Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13
    • DOI 10.1016/j.str.2004.07.015, PII S0969212604002849
    • D.L. Theobald, and D.S. Wuttke Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13 Structure 12 2004 1877 1879 (Pubitemid 39298970)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1877-1879
    • Theobald, D.L.1    Wuttke, D.S.2
  • 38
    • 15744372316 scopus 로고    scopus 로고
    • Extended DNA binding site in Pot1 broadens sequence specificity to allow recognition of heterogeneous fission yeast telomeres
    • DOI 10.1074/jbc.M414511200
    • K.M. Trujillo, J.T. Bunch, and P. Baumann Extended DNA binding site in Pot1 broadens sequence specificity to allow recognition of heterogeneous fission yeast telomeres J. Biol. Chem. 280 2005 9119 9128 (Pubitemid 40409606)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9119-9128
    • Trujillo, K.M.1    Bunch, J.T.2    Baumann, P.3
  • 39
    • 84859952473 scopus 로고    scopus 로고
    • Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site
    • C.T. Valley, D.F. Porter, C. Qiu, Z.T. Campbell, T.M.T. Hall, and M. Wickens Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site Proc. Natl. Acad. Sci. USA 109 2012 6054 6059
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6054-6059
    • Valley, C.T.1    Porter, D.F.2    Qiu, C.3    Campbell, Z.T.4    Hall, T.M.T.5    Wickens, M.6
  • 41
    • 77954262905 scopus 로고    scopus 로고
    • 3V: Cavity, channel and cleft volume calculator and extractor
    • WEB SERVER ISSUE
    • N.R. Voss, and M. Gerstein 3V: cavity, channel and cleft volume calculator and extractor Nucleic Acids Res. 38 Web Server issue 2010 W555 W562
    • (2010) Nucleic Acids Res. , vol.38
    • Voss, N.R.1    Gerstein, M.2
  • 42
    • 73949159967 scopus 로고    scopus 로고
    • Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein
    • Y. Wang, L. Opperman, M. Wickens, and T.M.T. Hall Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein Proc. Natl. Acad. Sci. USA 106 2009 20186 20191
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20186-20191
    • Wang, Y.1    Opperman, L.2    Wickens, M.3    Hall, T.M.T.4
  • 45
    • 34250851687 scopus 로고    scopus 로고
    • LOMETS: A local meta-threading-server for protein structure prediction
    • DOI 10.1093/nar/gkm251
    • S. Wu, and Y. Zhang LOMETS: a local meta-threading-server for protein structure prediction Nucleic Acids Res. 35 2007 3375 3382 (Pubitemid 47073600)
    • (2007) Nucleic Acids Research , vol.35 , Issue.10 , pp. 3375-3382
    • Wu, S.1    Zhang, Y.2


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