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Volumn 46, Issue 5, 2011, Pages 409-435

Structural anatomy of telomere OB proteins

Author keywords

Allostery; Intrinsically disordered protein regions; Molecular recognition; NMR; OB fold; Single stranded DNA binding proteins; Telomere structural biology; X ray crystallography

Indexed keywords

DNA BINDING PROTEIN; DNA POLYMERASE; OB PROTEIN; REPLICATION FACTOR A; SINGLE STRANDED DNA; TELOMERASE; UNCLASSIFIED DRUG;

EID: 80053464451     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2011.609295     Document Type: Review
Times cited : (28)

References (104)
  • 1
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • DOI 10.1093/bioinformatics/bti263
    • Abascal F, Zardoya R, Posada D. 2005. ProtTest: selection of best-ft models of protein evolution. Bioinformatics 21:2104-2105. (Pubitemid 40668057)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 2
    • 0038473989 scopus 로고    scopus 로고
    • OB-fold: Growing bigger with functional consistency
    • DOI 10.2174/1389203033487207
    • Agrawal V, Kishan K V. 2003. OB-fold: growing bigger with functional consistency. Curr Protein Pept Sci 4:195-206. (Pubitemid 36656733)
    • (2003) Current Protein and Peptide Science , vol.4 , Issue.3 , pp. 195-206
    • Agrawal, V.1    Kishan, K.V.R.2
  • 3
    • 1342309210 scopus 로고    scopus 로고
    • Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference
    • DOI 10.1093/bioinformatics/btg427
    • Altekar G, Dwarkadas S, Huelsenbeck JP, Ronquist F. 2004. Parallel Metropolis coupled Markov chain Monte Carlo for Bayesian phylogenetic inference. Bioinformatics 20:407-415. (Pubitemid 38262773)
    • (2004) Bioinformatics , vol.20 , Issue.3 , pp. 407-415
    • Altekar, G.1    Dwarkadas, S.2    Huelsenbeck, J.P.3    Ronquist, F.4
  • 4
    • 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
    • Anderson EM, Halsey WA, Wuttke DS. 2003. Site-directed muta-genesis reveals the thermodynamic requirements for single-stranded DNA recognition by the telomere-binding protein Cdc13. Biochemistry 42:3751-3758. (Pubitemid 36402668)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3751-3758
    • Anderson, E.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 5
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • DOI 10.1016/S0959-440X(02)00392-5
    • Arcus V. 2002. OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr Opin Struct Biol 12: 794-801. (Pubitemid 36009497)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 794-801
    • Arcus, V.1
  • 6
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • DOI 10.1126/science.1060036
    • Baumann P, Cech TR. 2001. Pot1, the putative telomere end-binding protein in fssion yeast and humans. Science 292:1171-1175. (Pubitemid 32440940)
    • (2001) Science , vol.292 , Issue.5519 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 7
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2.0 A resolution
    • Bennett MJ, Choe S, Eisenberg D. 1994. Refned structure of dimeric diphtheria toxin at 2.0 A resolution. Protein Sci 3:1444-1463. (Pubitemid 24314464)
    • (1994) Protein Science , vol.3 , Issue.9 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 8
    • 0033575671 scopus 로고    scopus 로고
    • The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding
    • DOI 10.1093/emboj/18.16.4498
    • Bochkarev A, Bochkareva E, Frappier L, Edwards AM. 1999. The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. EMBO J 18:4498-4504. (Pubitemid 29391259)
    • (1999) EMBO Journal , vol.18 , Issue.16 , pp. 4498-4504
    • Bochkarev, A.1    Bochkareva, E.2    Frappier, L.3    Edwards, A.M.4
  • 9
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • DOI 10.1038/385176a0
    • Bochkarev A, Pfuetzner RA, Edwards AM, Frappier L. 1997. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385:176-181. (Pubitemid 27034221)
    • (1997) Nature , vol.385 , Issue.6612 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 10
    • 0035253862 scopus 로고    scopus 로고
    • Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding
    • DOI 10.1093/emboj/20.3.612
    • Bochkareva E, Belegu V, Korolev S, Bochkarev A. 2001. Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding. EMBO J 20:612-618. (Pubitemid 32126996)
    • (2001) EMBO Journal , vol.20 , Issue.3 , pp. 612-618
    • Bochkareva, E.1    Belegu, V.2    Korolev, S.3    Bochkarev, A.4
  • 12
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • DOI 10.1093/emboj/21.7.1855
    • Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A. 2002. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO J 21:1855-1863. (Pubitemid 34614641)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1855-1863
    • Bochkareva, E.1    Korolev, S.2    Lees-Miller, S.P.3    Bochkarev, A.4
  • 13
    • 0025950546 scopus 로고
    • Replication factor-A from Saccharomyces cerevisiae is encoded by three essential genes coordinately expressed at S phase
    • Brill SJ, Stillman B. 1991. Replication factor-A from Saccharomyces cerevisiae is encoded by three essential genes coordinately expressed at S phase. Genes Dev 5:1589-1600. (Pubitemid 21906064)
    • (1991) Genes and Development , vol.5 , Issue.9 , pp. 1589-1600
    • Brill, S.J.1    Stillman, B.2
  • 14
    • 33845983694 scopus 로고    scopus 로고
    • Structural reorganization and the cooperative binding of single-stranded telomere DNA in Sterkiella nova
    • DOI 10.1074/jbc.M607749200
    • Buczek P, Horvath MP. 2006a. Structural reorganization and the cooperative binding of single-stranded telomere DNA in Sterkiella nova. J Biol Chem 281:40124-40134. (Pubitemid 46041817)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 40124-40134
    • Buczek, P.1    Horvath, M.P.2
  • 15
    • 33745176269 scopus 로고    scopus 로고
    • Thermodynamic Characterization of Binding Oxytricha nova Single Strand Telomere DNA with the Alpha Protein N-terminal Domain
    • DOI 10.1016/j.jmb.2006.02.082, PII S0022283606004761
    • Buczek P, Horvath MP. 2006b. Termodynamic characterization of binding Oxytricha nova single strand telomere DNA with the alpha protein N-terminal domain. J Mol Biol 359:1217-1234. (Pubitemid 43903488)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.5 , pp. 1217-1234
    • Buczek, P.1    Horvath, M.P.2
  • 16
  • 17
    • 65549148649 scopus 로고    scopus 로고
    • A DNA polymerase-{alpha}{middle dot}primase cofactor with homology to replication protein A-32 regulates DNA replication in mammalian cells
    • Casteel DE, Zhuang S, Zeng Y, Perrino FW, Boss GR, Goulian M, Pilz RB. 2009. A DNA polymerase-{alpha}{middle dot}primase cofactor with homology to replication protein A-32 regulates DNA replication in mammalian cells. J Biol Chem 284:5807-5818.
    • (2009) J Biol Chem , vol.284 , pp. 5807-5818
    • Casteel, D.E.1    Zhuang, S.2    Zeng, Y.3    Perrino, F.W.4    Boss, G.R.5    Goulian, M.6    Pilz, R.B.7
  • 18
    • 0035115859 scopus 로고    scopus 로고
    • Cdc13 both positively and negatively regulates telomere replication
    • DOI 10.1101/gad.861001
    • Chandra A, Hughes TR, Nugent CI, Lundblad V. 2001. Cdc13 both positively and negatively regulates telomere replication. Genes Dev 15:404-414. (Pubitemid 32187002)
    • (2001) Genes and Development , vol.15 , Issue.4 , pp. 404-414
    • Chandra, A.1    Hughes, T.R.2    Nugent, C.I.3    Lundblad, V.4
  • 19
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: A protein structure and structural feature prediction server
    • DOI 10.1093/nar/gki396
    • Cheng J, Randall AZ, Sweredoski MJ, Baldi P. 2005. SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res 33:W72-W76. (Pubitemid 44529882)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 20
    • 0041989705 scopus 로고    scopus 로고
    • Sequence-specific and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein α subunit
    • DOI 10.1021/bi0273718
    • Classen S, Lyons D, Cech TR, Schultz SC. 2003. Sequence-specifc and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein alpha subunit. Biochemistry 42:9269-9277. (Pubitemid 36959234)
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9269-9277
    • Classen, S.1    Lyons, D.2    Cech, T.R.3    Schultz, S.C.4
  • 21
    • 0035861983 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein α subunit both uncomplexed and complexed with telomeric ssDNA
    • DOI 10.1006/jmbi.2000.5191
    • Classen S, Ruggles JA, Schultz SC. 2001. Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA. J Mol Biol 314:1113-1125. (Pubitemid 34073074)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.5 , pp. 1113-1125
    • Classen, S.1    Ruggles, J.A.2    Schultz, S.C.3
  • 22
    • 42049083762 scopus 로고    scopus 로고
    • Deciphering the mechanism of thermodynamic accommodation of telomeric oligonucleotide sequences by the Schizosaccharomyces pombe protection of telomeres 1 (Pot1pN) protein
    • DOI 10.1021/bi701778x
    • Croy JE, Fast JL, Grimm NE, Wuttke DS. 2008. Deciphering the mechanism of thermodynamic accommodation of telomeric oligonucleotide sequences by the Schizosaccharomyces pombe protection of telomeres 1 (Pot1pN) protein. Biochemistry 47: 4345-4358. (Pubitemid 351522083)
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4345-4358
    • Croy, J.E.1    Fast, J.L.2    Grimm, N.E.3    Wuttke, D.S.4
  • 23
    • 33745906967 scopus 로고    scopus 로고
    • 1-389
    • DOI 10.1016/j.jmb.2006.06.002, PII S0022283606006930
    • Croy JE, Podell ER, Wuttke DS. 2006. A new model for Schizo-saccharomyces pombe telomere recognition: the telomeric single-stranded DNA-binding activity of Pot11-389. J Mol Biol 361:80-93. (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
  • 24
    • 33747751221 scopus 로고    scopus 로고
    • Themes in ssDNA recognition by telomere-end protection proteins
    • DOI 10.1016/j.tibs.2006.07.004, PII S0968000406001952
    • Croy JE, Wuttke DS. 2006. Temes in ssDNA recognition by telomere-end protection proteins. Trends Biochem Sci 31:516-525. (Pubitemid 44279982)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.9 , pp. 516-525
    • Croy, J.E.1    Wuttke, D.S.2
  • 25
    • 71149093724 scopus 로고    scopus 로고
    • How telomeres solve the end-protection problem
    • De Lange T. 2009. How telomeres solve the end-protection problem. Science 326:948-952.
    • (2009) Science , vol.326 , pp. 948-952
    • De Lange, T.1
  • 26
    • 35748971020 scopus 로고    scopus 로고
    • Structure of the Full-length Human RPA14/32 Complex Gives Insights into the Mechanism of DNA Binding and Complex Formation
    • DOI 10.1016/j.jmb.2007.09.074, PII S0022283607012867
    • Deng X, Habel JE, Kabaleeswaran V, Snell EH, Wold MS, Borgstahl GE. 2007. Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation. J Mol Biol 374:865-876. (Pubitemid 350052093)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 865-876
    • Deng, X.1    Habel, J.E.2    Kabaleeswaran, V.3    Snell, E.H.4    Wold, M.S.5    Borgstahl, G.E.O.6
  • 27
    • 31044455231 scopus 로고    scopus 로고
    • Identification of the determinants for the specific recognition of single-strand telomeric DNA by Cdc13
    • DOI 10.1021/bi0512703
    • Eldridge AM, Halsey WA, Wuttke DS. 2006. Identifcation of the determinants for the specifc recognition of single-strand telomeric DNA by Cdc13. Biochemistry 45:871-879. (Pubitemid 43122251)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 871-879
    • Eldridge, A.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 28
    • 41149125565 scopus 로고    scopus 로고
    • Probing the mechanism of recognition of ssDNA by the Cdc13-DBD
    • DOI 10.1093/nar/gkn017
    • Eldridge AM, Wuttke DS. 2008. Probing the mechanism of recognition of ssDNA by the Cdc13-DBD. Nucleic Acids Res 36:1624-1633. (Pubitemid 351426114)
    • (2008) Nucleic Acids Research , vol.36 , Issue.5 , pp. 1624-1633
    • Eldridge, A.M.1    Wuttke, D.S.2
  • 29
    • 1842311742 scopus 로고
    • Cellular factors required for multiple stages of SV40 DNA replication in vitro
    • Fairman MP, Stillman B. 1988. Cellular factors required for multiple stages of SV40 DNA replication in vitro. EMBO J 7:1211-1218.
    • (1988) EMBO J , vol.7 , pp. 1211-1218
    • Fairman, M.P.1    Stillman, B.2
  • 31
    • 0027168268 scopus 로고
    • Oxytricha telomere-binding protein: Separable DNA-binding and dimerization domains of the α-subunit
    • Fang G, Gray JT, Cech TR. 1993. Oxytricha telomere-binding protein: separable DNA-binding and dimerization domains of the alpha-subunit. Genes Dev 7:870-882. (Pubitemid 23163590)
    • (1993) Genes and Development , vol.7 , Issue.5 , pp. 870-882
    • Fang, G.1    Gray, J.T.2    Cech, T.R.3
  • 32
    • 33749134033 scopus 로고    scopus 로고
    • A dynamic model for replication protein A (RPA) function in DNA processing pathways
    • DOI 10.1093/nar/gkl550
    • Fanning E, Klimovich V, Nager AR. 2006. A dynamic model for replication protein A (RPA) function in DNA processing pathways. Nucleic Acids Res 34:4126-4137. (Pubitemid 44542191)
    • (2006) Nucleic Acids Research , vol.34 , Issue.15 , pp. 4126-4137
    • Fanning, E.1    Klimovich, V.2    Nager, A.R.3
  • 33
    • 77954589779 scopus 로고    scopus 로고
    • Oligonucleotide/oligosaccharide-binding fold proteins: A growing family of genome guardians
    • Flynn RL, Zou L. 2010. Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians. Crit Rev Biochem Mol Biol 45:266-275.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 266-275
    • Flynn, R.L.1    Zou, L.2
  • 36
    • 0023037564 scopus 로고
    • Telomere proteins: Specific recognition and protection of the natural termini of Oxytricha macronuclear DNA
    • Gottschling DE, Zakian VA. 1986. Telomere proteins: specifc recognition and protection of the natural termini of Oxytricha macronuclear DNA. Cell 47:195-205. (Pubitemid 17181539)
    • (1986) Cell , vol.47 , Issue.2 , pp. 195-205
    • Gottschling, D.E.1    Zakian, V.A.2
  • 37
    • 0025329799 scopus 로고
    • The mechanism of action of an accessory protein for DNA polymerase alpha/primase
    • Goulian M, Heard CJ. 1990. The mechanism of action of an accessory protein for DNA polymerase alpha/primase. J Biol Chem 265: 13231-13239.
    • (1990) J Biol Chem , vol.265 , pp. 13231-13239
    • Goulian, M.1    Heard, C.J.2
  • 38
    • 0025017971 scopus 로고
    • Discontinuous DNA synthesis by purifed mammalian proteins
    • Goulian M, Richards SH, Heard CJ, Bigsby BM. 1990. Discontinuous DNA synthesis by purifed mammalian proteins. J Biol Chem 265: 18461-18471.
    • (1990) J Biol Chem , vol.265 , pp. 18461-18471
    • Goulian, M.1    Richards, S.H.2    Heard, C.J.3    Bigsby, B.M.4
  • 39
    • 0035282781 scopus 로고    scopus 로고
    • Ten1 functions in telomere end protection and length regulation in association with Stn1 and Cdc13
    • DOI 10.1093/emboj/20.5.1173
    • Grandin N, Damon C, Charbonneau M. 2001. Ten1 functions in telomere end protection and length regulation in association with Stn1 and Cdc13. EMBO J 20:1173-1183. (Pubitemid 32186807)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1173-1183
    • Grandin, N.1    Damon, C.2    Charbonneau, M.3
  • 40
    • 0031029001 scopus 로고    scopus 로고
    • Stn1, a new Saccharomyces cerevisiae protein, is implicated in telomere size regulation in association with CDc13
    • Grandin N, Reed SI, Charbonneau M. 1997. Stn1, a new Saccharomyces cerevisiae protein, is implicated in telomere size regulation in association with Cdc13. Genes Dev 11:512-527. (Pubitemid 27097649)
    • (1997) Genes and Development , vol.11 , Issue.4 , pp. 512-527
    • Grandin, N.1    Reed, S.I.2    Charbonneau, M.3
  • 41
    • 44449117551 scopus 로고    scopus 로고
    • Protein disorder prediction at multiple levels of sensitivity and specifcity
    • Hecker J, Yang JY, Cheng J. 2008. Protein disorder prediction at multiple levels of sensitivity and specifcity. BMC Genomics 9 Suppl 1:S9.
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL.
    • Hecker, J.1    Yang, J.Y.2    Cheng, J.3
  • 42
    • 55349087385 scopus 로고    scopus 로고
    • Evolution of telomere binding proteins
    • Tomaska, L., and Nosek, J., Eds., Austin, TX, Landes Bioscience
    • Horvath MP, Evolution of telomere binding proteins, in Origin and Evolution of Telomeres, Tomaska, L., and Nosek, J., Eds., Austin, TX, Landes Bioscience, 2008a, 83-99.
    • (2008) Origin and Evolution of Telomeres , pp. 83-99
    • Horvath, M.P.1
  • 43
    • 77955973565 scopus 로고    scopus 로고
    • Single-stranded nucleic acid-binding proteins
    • Rice, P.A., and Correll, C.C., Eds., London, Royal Society of Chemistry
    • Horvath MP, Single-stranded nucleic acid-binding proteins, in Protein-Nucleic Acid Interactions: Structural Biology, Rice, P.A., and Correll, C.C., Eds., London, Royal Society of Chemistry, 2008b, 91-128.
    • (2008) Protein-Nucleic Acid Interactions: Structural Biology , pp. 91-128
    • Horvath, M.P.1
  • 44
    • 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
    • Horvath MP, Schweiker VL, Bevilacqua JM, Ruggles JA, Schultz SC. 1998. Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA. Cell 95:963-974. (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
  • 45
    • 1342264709 scopus 로고    scopus 로고
    • Interaction of Saccharomyces Cdc13p with Pol1p, Imp4p, Sir4p and Zds2p is involved in telomere replication, telomere maintenance and cell growth control
    • Hsu CL, Chen YS, Tsai SY, Tu PJ, Wang MJ, Lin JJ. 2004. Interaction of Saccharomyces Cdc13p with Pol1p, Imp4p, Sir4p and Zds2p is involved in telomere replication, telomere maintenance and cell growth control. Nucleic Acids Res 32:511-521.
    • (2004) Nucleic Acids Res , vol.32 , pp. 511-521
    • Hsu, C.L.1    Chen, Y.S.2    Tsai, S.Y.3    Tu, P.J.4    Wang, M.J.5    Lin, J.J.6
  • 46
    • 52649130704 scopus 로고    scopus 로고
    • Protein-protein interaction and quaternary structure
    • Janin J, Bahadur RP, Chakrabarti P. 2008. Protein-protein interaction and quaternary structure. Q Rev Biophys 41:133-180.
    • (2008) Q Rev Biophys , vol.41 , pp. 133-180
    • Janin, J.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 47
    • 0019568388 scopus 로고
    • All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus
    • Klobutcher LA, Swanton MT, Donini P, Prescott DM. 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
  • 48
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide S, Sidhu SS. 2009. The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem Biol 4:325-334.
    • (2009) ACS Chem Biol , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 49
    • 49549102657 scopus 로고    scopus 로고
    • Understanding mechanisms governing protein-protein interactions from synthetic binding interfaces
    • Kossiakof AA, Koide S. 2008. Understanding mechanisms governing protein-protein interactions from synthetic binding interfaces. Curr Opin Struct Biol 18:499-506.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 499-506
    • Kossiakof, A.A.1    Koide, S.2
  • 50
    • 77649317032 scopus 로고    scopus 로고
    • POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation
    • Latrick CM, Cech TR. 2010. POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation. EMBO J 29:924-933.
    • (2010) EMBO J , vol.29 , pp. 924-933
    • Latrick, C.M.1    Cech, T.R.2
  • 51
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • DOI 10.1093/molbev/msn067
    • Le SQ, Gascuel O. 2008. An improved general amino acid replacement matrix. Mol Biol Evol 25:1307-1320. (Pubitemid 351882003)
    • (2008) Molecular Biology and Evolution , vol.25 , Issue.7 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 52
    • 77952295829 scopus 로고    scopus 로고
    • Investigating the role of the Est3 protein in yeast telomere replication
    • Lee J, Mandell EK, Rao T, Wuttke DS, Lundblad V. 2010. Investigating the role of the Est3 protein in yeast telomere replication. Nucleic Acids Res 38:2279-2290.
    • (2010) Nucleic Acids Res , vol.38 , pp. 2279-2290
    • Lee, J.1    Mandell, E.K.2    Rao, T.3    Wuttke, D.S.4    Lundblad, V.5
  • 54
    • 0037058877 scopus 로고    scopus 로고
    • Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe
    • DOI 10.1021/bi026674z
    • Lei M, Baumann P, Cech TR. 2002. Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe. Biochemistry 41:14560-14568. (Pubitemid 35440269)
    • (2002) Biochemistry , vol.41 , Issue.49 , pp. 14560-14568
    • Lei, M.1    Baumann, P.2    Cech, T.R.3
  • 55
    • 0345304903 scopus 로고    scopus 로고
    • DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA
    • Lei M, Podell ER, Baumann P, Cech TR. 2003. DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA. Nature 426:198-203.
    • (2003) Nature , vol.426 , pp. 198-203
    • Lei, M.1    Podell, E.R.2    Baumann, P.3    Cech, T.R.4
  • 56
    • 12844265975 scopus 로고    scopus 로고
    • Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
    • Lei M, Podell ER, Cech TR. 2004. Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection. Nat Struct Mol Biol 11:1223-1229.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1223-1229
    • Lei, M.1    Podell, E.R.2    Cech, T.R.3
  • 57
    • 20144382152 scopus 로고    scopus 로고
    • Switching human telomerase on and off with hPOT1 protein in vitro
    • DOI 10.1074/jbc.M502212200
    • Lei M, Zaug AJ, Podell ER, Cech TR. 2005. Switching human telomerase on and of with hPOT1 protein in vitro. J Biol Chem 280:20449-20456. (Pubitemid 40776744)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20449-20456
    • Lei, M.1    Zaug, A.J.2    Podell, E.R.3    Cech, T.R.4
  • 58
    • 0034716904 scopus 로고    scopus 로고
    • Identifcation of human Rap1: Implications for telomere evolution
    • Li B, Oestreich S, de Lange T. 2000. Identifcation of human Rap1: implications for telomere evolution. Cell 101:471-483.
    • (2000) Cell , vol.101 , pp. 471-483
    • Li, B.1    Oestreich, S.2    De Lange, T.3
  • 59
    • 70350020161 scopus 로고    scopus 로고
    • Conservation of telomere protein complexes: Shufing through evolution
    • Linger BR, Price CM. 2009. Conservation of telomere protein complexes: shufing through evolution. Crit Rev Biochem Mol Biol 44:434-446.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , pp. 434-446
    • Linger, B.R.1    Price, C.M.2
  • 64
    • 0037023303 scopus 로고    scopus 로고
    • Conserved structure for single-stranded telomeric DNA recognition
    • DOI 10.1126/science.1068799
    • Mitton-Fry RM, Anderson EM, Hughes TR, Lundblad V, Wuttke DS. 2002. Conserved structure for single-stranded telomeric DNA recognition. Science 296:145-147. (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
  • 66
    • 70350031814 scopus 로고    scopus 로고
    • RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway
    • Miyake Y, Nakamura M, Nabetani A, Shimamura S, Tamura M, Yonehara S, Saito M, Ishikawa F. 2009. RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway. Mol Cell 36: 193-206.
    • (2009) Mol Cell , vol.36 , pp. 193-206
    • Miyake, Y.1    Nakamura, M.2    Nabetani, A.3    Shimamura, S.4    Tamura, M.5    Yonehara, S.6    Saito, M.7    Ishikawa, F.8
  • 67
    • 45549090631 scopus 로고    scopus 로고
    • Fission yeast pot1-Tpp1 protects telomeres and regulates telomere length
    • DOI 10.1126/science.1154819
    • Miyoshi T, Kanoh J, Saito M, Ishikawa F. 2008. Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science 320:1341-1344. (Pubitemid 351929470)
    • (2008) Science , vol.320 , Issue.5881 , pp. 1341-1344
    • Miyoshi, T.1    Kanoh, J.2    Saito, M.3    Ishikawa, F.4
  • 68
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin AG. 1993. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J 12:861-867. (Pubitemid 23095834)
    • (1993) EMBO Journal , vol.12 , Issue.3 , pp. 861-867
    • Murzin, A.G.1
  • 69
    • 76249110370 scopus 로고    scopus 로고
    • How telomeric protein POT1 avoids RNA to achieve specifcity for single-stranded DNA
    • Nandakumar J, Podell ER, Cech TR. 2010. How telomeric protein POT1 avoids RNA to achieve specifcity for single-stranded DNA. Proc Natl Acad Sci USA 107:651-656.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 651-656
    • Nandakumar, J.1    Podell, E.R.2    Cech, T.R.3
  • 71
    • 0036176232 scopus 로고    scopus 로고
    • Dimeric structure of the Oxytricha nova telomere end-binding protein α-subunit bound to ssDNA
    • DOI 10.1038/nsb761
    • Peersen OB, Ruggles JA, Schultz SC. 2002. Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA. Nat Struct Biol 9:182-187. (Pubitemid 34171309)
    • (2002) Nature Structural Biology , vol.9 , Issue.3 , pp. 182-187
    • Peersen, O.B.1    Ruggles, J.A.2    Schultz, S.C.3
  • 72
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • DOI 10.1016/S0092-8674(01)00226-4
    • Pennock E, Buckley K, Lundblad V. 2001. Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell 104:387-396. (Pubitemid 32206459)
    • (2001) Cell , vol.104 , Issue.3 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 73
    • 0025345912 scopus 로고
    • Telomere structure in Euplotes crassus: Characterization of DNA-protein interactions and isolation of a telomere-binding protein
    • Price CM. 1990. Telomere structure in Euplotes crassus: characterization of DNA-protein interactions and isolation of a telomere-binding protein. Mol Cell Biol 10:3421-3431.
    • (1990) Mol Cell Biol , vol.10 , pp. 3421-3431
    • Price, C.M.1
  • 75
    • 0023433713 scopus 로고
    • Telomeric DNA-protein interactions of Oxytricha macronuclear DNA
    • Price CM, Cech TR. 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
  • 76
    • 0024551991 scopus 로고
    • Properties of the telomeric DNA-binding protein from Oxytricha nova
    • DOI 10.1021/bi00428a053
    • Price CM, Cech TR. 1989. Properties of the telomeric DNA-binding protein from Oxytricha nova. Biochemistry 28:769-774. (Pubitemid 19047116)
    • (1989) Biochemistry , vol.28 , Issue.2 , pp. 769-774
    • Price, C.M.1    Cech, T.R.2
  • 77
    • 51049092483 scopus 로고    scopus 로고
    • Distinct roles for yeast Stn1 in telomere capping and telomerase inhibition
    • Puglisi A, Bianchi A, Lemmens L, Damay P, Shore D. 2008. Distinct roles for yeast Stn1 in telomere capping and telomerase inhibition. EMBO J 27:2328-2339.
    • (2008) EMBO J , vol.27 , pp. 2328-2339
    • Puglisi, A.1    Bianchi, A.2    Lemmens, L.3    Damay, P.4    Shore, D.5
  • 78
    • 0034661246 scopus 로고    scopus 로고
    • The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated Est1 protein
    • Qi H, Zakian VA. 2000. The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein. Genes Dev 14:1777-1788. (Pubitemid 30602996)
    • (2000) Genes and Development , vol.14 , Issue.14 , pp. 1777-1788
    • Qi, H.1    Zakian, V.A.2
  • 79
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger MP, Bennett MJ, Eisenberg D. 1997. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv Protein Chem 50:61-122. (Pubitemid 27449486)
    • (1997) Advances in Protein Chemistry , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 80
    • 0036306236 scopus 로고    scopus 로고
    • On the role of electrostatic interactions in the design of protein-protein interfaces
    • DOI 10.1016/S0022-2836(02)00030-X
    • Sheinerman FB, Honig B. 2002. On the role of electrostatic interactions in the design of protein-protein interfaces. J Mol Biol 318:161-177. (Pubitemid 34729393)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.1 , pp. 161-177
    • Sheinerman, F.B.1    Honig, B.2
  • 82
    • 85027917185 scopus 로고    scopus 로고
    • Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase alpha
    • Sun J, Yang Y, Wan K, Mao N, Yu TY, Lin YC, Dezwaan DC, Freeman BC, Lin JJ, Lue NF and Lei M. 2011. Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase alpha. Cell Res 21:258-274.
    • (2011) Cell Res , vol.21 , pp. 258-274
    • Sun, J.1    Yang, Y.2    Wan, K.3    Mao, N.4    Yu, T.Y.5    Lin, Y.C.6    Dezwaan, D.C.7    Freeman, B.C.8    Lin, J.J.9    Lue, N.F.10    Lei, M.11
  • 85
    • 23944502886 scopus 로고    scopus 로고
    • Telomere maintenance, function and evolution: The yeast paradigm
    • DOI 10.1007/s10577-005-0999-0
    • Teixeira MT, Gilson E. 2005. Telomere maintenance, function and evolution: the yeast paradigm. Chromosome Res 13:535-548. (Pubitemid 41205636)
    • (2005) Chromosome Research , vol.13 , Issue.5 , pp. 535-548
    • Teixeira, M.T.1    Gilson, E.2
  • 86
    • 0042972659 scopus 로고    scopus 로고
    • Homology among telomeric end-protection proteins
    • DOI 10.1016/S0969-2126(03)00183-7
    • Teobald DL, Cervantes RB, Lundblad V, Wuttke DS. 2003a. Homology among telomeric end-protection proteins. Structure 11:1049-1050. (Pubitemid 37103066)
    • (2003) Structure , vol.11 , Issue.9 , pp. 1049-1050
    • Theobald, D.L.1    Cervantes, R.B.2    Lundblad, V.3    Wuttke, D.S.4
  • 88
    • 0042035638 scopus 로고    scopus 로고
    • Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes
    • DOI 10.1093/emboj/cdg415
    • Teobald DL, Schultz SC. 2003. Nucleotide shufing and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes. EMBO J 22:4314-4324. (Pubitemid 37021758)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4314-4324
    • Theobald, D.L.1    Schultz, S.C.2
  • 89
    • 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
    • Teobald DL, Wuttke DS. 2004. Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13. Structure 12:1877-1879. (Pubitemid 39298970)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1877-1879
    • Theobald, D.L.1    Wuttke, D.S.2
  • 90
    • 27744562914 scopus 로고    scopus 로고
    • Divergent evolution within protein superfolds inferred from profile-based phylogenetics
    • DOI 10.1016/j.jmb.2005.08.071, PII S002228360501051X
    • Teobald DL, Wuttke DS. 2005. Divergent evolution within protein superfolds inferred from profle-based phylogenetics. J Mol Biol 354:722-737. (Pubitemid 41628288)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.3 , pp. 722-737
    • Theobald, D.L.1    Wuttke, D.S.2
  • 91
    • 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
    • Trujillo KM, Bunch JT, Baumann P. 2005. Extended DNA binding site in Pot1 broadens sequence specifcity to allow recognition of heterogeneous fssion yeast telomeres. J Biol Chem 280:9119-9128. (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
  • 92
    • 34250841785 scopus 로고    scopus 로고
    • Replication and protection of telomeres
    • DOI 10.1038/nature05976, PII NATURE05976
    • Verdun RE, Karlseder J. 2007. Replication and protection of telomeres. Nature 447:924-931. (Pubitemid 46975759)
    • (2007) Nature , vol.447 , Issue.7147 , pp. 924-931
    • Verdun, R.E.1    Karlseder, J.2
  • 93
    • 77954262905 scopus 로고    scopus 로고
    • 3V: Cavity, channel and cleft volume calculator and extractor
    • Voss NR, Gerstein M. 2010. 3V: cavity, channel and cleft volume calculator and extractor. Nucleic Acids Res 38:W555-W562.
    • (2010) Nucleic Acids Res , vol.38
    • Voss, N.R.1    Gerstein, M.2
  • 94
    • 70350001509 scopus 로고    scopus 로고
    • OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation
    • Wan M, Qin J, Songyang Z, Liu D. 2009. OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation. J Biol Chem 284: 26725-26731.
    • (2009) J Biol Chem , vol.284 , pp. 26725-26731
    • Wan, M.1    Qin, J.2    Songyang, Z.3    Liu, D.4
  • 95
    • 33846691378 scopus 로고    scopus 로고
    • The POT1-TPP1 telomere complex is a telomerase processivity factor
    • DOI 10.1038/nature05454, PII NATURE05454
    • Wang F, Podell ER, Zaug AJ, Yang Y, Baciu P, Cech TR, Lei M. 2007. The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature 445:506-510. (Pubitemid 46197626)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 506-510
    • Wang, F.1    Podell, E.R.2    Zaug, A.J.3    Yang, Y.4    Baciu, P.5    Cech, T.R.6    Lei, M.7
  • 96
    • 70350032208 scopus 로고    scopus 로고
    • The CST complex and telomere maintenance: The exception becomes the rule
    • Wellinger RJ. 2009. The CST complex and telomere maintenance: the exception becomes the rule. Mol Cell 36:168-169.
    • (2009) Mol Cell , vol.36 , pp. 168-169
    • Wellinger, R.J.1
  • 97
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • DOI 10.1146/annurev.biochem.66.1.61
    • Wold MS. 1997. Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu Rev Biochem 66:61-92. (Pubitemid 27274652)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 98
    • 0023992803 scopus 로고
    • Purifcation and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA
    • Wold MS, Kelly T. 1988. Purifcation and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA. Proc Natl Acad Sci USA 85:2523-2527.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2523-2527
    • Wold, M.S.1    Kelly, T.2
  • 99
    • 33846692105 scopus 로고    scopus 로고
    • TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase
    • DOI 10.1038/nature05469, PII NATURE05469
    • Xin H, Liu D, Wan M, Safari A, Kim H, Sun W, O'Connor MS, Songyang Z. 2007. TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature 445:559-562. (Pubitemid 46197638)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 559-562
    • Xin, H.1    Liu, D.2    Wan, M.3    Safari, A.4    Kim, H.5    Sun, W.6    O'Connor, M.S.7    Songyang, Z.8
  • 100
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai CJ, Nussinov R. 1997. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 10:999-1012. (Pubitemid 28004646)
    • (1997) Protein Engineering , vol.10 , Issue.9 , pp. 999-1012
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 102
    • 80053464570 scopus 로고    scopus 로고
    • Telomerase and retrotrans-posons: Reverse transcriptases tat shaped genomes special feature sackler colloquium: Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA
    • (In Press)
    • Yen WF, Chico L, Lei M, Lue NF. 2011. Telomerase and Retrotrans-posons: Reverse Transcriptases Tat Shaped Genomes Special Feature Sackler Colloquium: Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA. Proc Natl Acad Sci USA (In Press).
    • (2011) Proc Natl Acad Sci USA
    • Yen, W.F.1    Chico, L.2    Lei, M.3    Lue, N.F.4
  • 103
    • 51349100639 scopus 로고    scopus 로고
    • A proposed OB-fold with a protein-interaction surface in Candida albicans telomerase protein Est3
    • Yu EY, Wang F, Lei M, Lue NF. 2008. A proposed OB-fold with a protein-interaction surface in Candida albicans telomerase protein Est3. Nat Struct Mol Biol 15:985-989.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 985-989
    • Yu, E.Y.1    Wang, F.2    Lei, M.3    Lue, N.F.4
  • 104
    • 77949382591 scopus 로고    scopus 로고
    • Functional interaction between telomere protein TPP1 and telomerase
    • Zaug AJ, Podell ER, Nandakumar J, Cech TR. 2010. Functional interaction between telomere protein TPP1 and telomerase. Genes Dev 24:613-622.
    • (2010) Genes Dev , vol.24 , pp. 613-622
    • Zaug, A.J.1    Podell, E.R.2    Nandakumar, J.3    Cech, T.R.4


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