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Volumn 24, Issue 5, 2004, Pages 2091-2102

Cell Cycle Localization, Dimerization, and Binding Domain Architecture of the Telomere Protein cPot1

Author keywords

[No Author keywords available]

Indexed keywords

CPOT1 PROTEIN; DNA; DNA BINDING PROTEIN; G STRAND DNA; OLIGONUCLEOTIDE; OLIGOSACCHARIDE; SINGLE STRANDED DNA; TELOMERE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 1342282906     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.5.2091-2102.2004     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 0036798283 scopus 로고    scopus 로고
    • Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13
    • Anderson, E. M., W. A. Halsey, and D. S. Wuttke. 2002. Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13. Nucleic Acids Res. 30:4305-4313.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4305-4313
    • Anderson, E.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 2
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel, P., C. T. Chien, R. Sternglanz, and S. Fields. 1993. Elimination of false positives that arise in using the two-hybrid system. BioTechniques 14:920-924.
    • (1993) BioTechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 3
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • Baumann, P., and T. R. Cech. 2001. Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292:1171-1175.
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 4
    • 0036840361 scopus 로고    scopus 로고
    • Human Pot1 (protection of telomeres) protein: Cytolocalization, gene structure, and alternative splicing
    • Baumann, P., E. Podell, and T. R. Cech. 2002. Human Pot1 (protection of telomeres) protein: cytolocalization, gene structure, and alternative splicing. Mol. Cell. Biol. 22:8079-8087.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8079-8087
    • Baumann, P.1    Podell, E.2    Cech, T.R.3
  • 6
    • 0035929353 scopus 로고    scopus 로고
    • Switching and signaling at the telomere
    • Blackburn, E. H. 2001. Switching and signaling at the telomere. Cell 106:661-673.
    • (2001) Cell , vol.106 , pp. 661-673
    • Blackburn, E.H.1
  • 7
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., R. A. Pfuetzner, A. M. Edwards, and L. Frappier. 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
  • 8
    • 0037148270 scopus 로고    scopus 로고
    • New ways not to make ends meet: Telomerase, DNA damage proteins and heterochromatin
    • Chan, S. W., and E. H. Blackburn. 2002. New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin. Oncogene 21:553-563.
    • (2002) Oncogene , vol.21 , pp. 553-563
    • Chan, S.W.1    Blackburn, E.H.2
  • 9
    • 0035115859 scopus 로고    scopus 로고
    • Cdc13 both positively and negatively regulates telomere replication
    • Chandra, A., T. R. Hughes, C. I. Nugent, and V. Lundblad. 2001. Cdc13 both positively and negatively regulates telomere replication. Genes Dev. 15:404-414.
    • (2001) Genes Dev. , vol.15 , pp. 404-414
    • Chandra, A.1    Hughes, T.R.2    Nugent, C.I.3    Lundblad, V.4
  • 10
    • 0041989705 scopus 로고    scopus 로고
    • Sequence-specific and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein alpha subunit
    • Classen, S., D. Lyons, T. R. Cech, and S. C. Schultz. 2003. Sequence-specific and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein alpha subunit. Biochemistry 42:9269-9277.
    • (2003) Biochemistry , vol.42 , pp. 9269-9277
    • Classen, S.1    Lyons, D.2    Cech, T.R.3    Schultz, S.C.4
  • 11
    • 0035861983 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA
    • Classen, S., J. A. Ruggles, and S. C. Schultz. 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. Bio. 314:1113-1125.
    • (2001) J. Mol. Bio. , vol.314 , pp. 1113-1125
    • Classen, S.1    Ruggles, J.A.2    Schultz, S.C.3
  • 13
    • 0032560121 scopus 로고    scopus 로고
    • Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination
    • Cooper, J. P., Y. Watanabe, and P. Nurse. 1998. Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination. Nature 392:828-831.
    • (1998) Nature , vol.392 , pp. 828-831
    • Cooper, J.P.1    Watanabe, Y.2    Nurse, P.3
  • 14
    • 0037148277 scopus 로고    scopus 로고
    • Protection of mammalian telomeres
    • de Lange, T. 2002. Protection of mammalian telomeres. Oncogene 21:532-540.
    • (2002) Oncogene , vol.21 , pp. 532-540
    • De Lange, T.1
  • 15
    • 0037954529 scopus 로고    scopus 로고
    • Vertebrate tankyrase domain structure and sterile alpha motif (SAM)-mediated multimerization
    • De Rycker, M., R. N. Venkatesan, C. Wei, and C. M. Price. 2003. Vertebrate tankyrase domain structure and sterile alpha motif (SAM)-mediated multimerization. Biochem. J. 372:87-96.
    • (2003) Biochem. J. , vol.372 , pp. 87-96
    • De Rycker, M.1    Venkatesan, R.N.2    Wei, C.3    Price, C.M.4
  • 16
    • 0033767689 scopus 로고    scopus 로고
    • Positive and negative regulation of telomerase access to the telomere
    • Evans, S. K., and V. Lundblad. 2000. Positive and negative regulation of telomerase access to the telomere. J. Cell Sci. 113:3357-3364.
    • (2000) J. Cell Sci. , vol.113 , pp. 3357-3364
    • Evans, S.K.1    Lundblad, V.2
  • 17
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall, L., L. Chapman, H. Moss, T. de Lange, and D. Rhodes. 2001. Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol. Cell 8:351-361.
    • (2001) Mol. Cell , vol.8 , pp. 351-361
    • Fairall, L.1    Chapman, L.2    Moss, H.3    De Lange, T.4    Rhodes, D.5
  • 18
    • 0002952287 scopus 로고
    • Telomere proteins
    • E. H. Blackburn and C. W. Greider (ed.). Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • Fang, G., and T. R. Cech. 1995. Telomere proteins, p. 69-107. In E. H. Blackburn and C. W. Greider (ed.), Telomeres. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • (1995) Telomeres , pp. 69-107
    • Fang, G.1    Cech, T.R.2
  • 19
    • 0028822203 scopus 로고
    • Single-stranded DNA arising at telomeres in cdcl3 mutants may constitute a specific signal for the RAD9 checkpoint
    • Garvik, B., M. Carson, and L. Hartwell. 1995. Single-stranded DNA arising at telomeres in cdcl3 mutants may constitute a specific signal for the RAD9 checkpoint. Mol. Cell. Biol. 15:6128-6138.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6128-6138
    • Garvik, B.1    Carson, M.2    Hartwell, L.3
  • 20
    • 0032562649 scopus 로고    scopus 로고
    • TRF1 promotes parallel pairing of telomeric tracts in vitro
    • Griffith, J., A. Bianchi, and T. de Lange. 1998. TRF1 promotes parallel pairing of telomeric tracts in vitro. J. Mol. Biol. 278:79-88.
    • (1998) J. Mol. Biol. , vol.278 , pp. 79-88
    • Griffith, J.1    Bianchi, A.2    De Lange, T.3
  • 22
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S. M., R. Sternglanz, P. F. Cheng, and H. Weintraub. 1995. Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15:3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 23
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • Horvath, M. P., V. L. Schweiker, J. M. Bevilacqua, J. A. Ruggles, and S. C. Schultz. 1998. Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA. Cell 95:963-974.
    • (1998) Cell , vol.95 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 24
    • 0034733606 scopus 로고    scopus 로고
    • Telomere shortening is proportional to the size of the 3′ G-rich telomeric overhang
    • Huffman, K. E., S. D. Levene, V. M. Tesmer, J. W. Shay, and W. E. Wright. 2000. Telomere shortening is proportional to the size of the 3′ G-rich telomeric overhang. J. Biol. Chem. 275:19719-19722.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19719-19722
    • Huffman, K.E.1    Levene, S.D.2    Tesmer, V.M.3    Shay, J.W.4    Wright, W.E.5
  • 25
    • 0034612253 scopus 로고    scopus 로고
    • Identification of the single-strand telomeric DNA binding domain of the Saccharomyces cerevisiae Cdc13 protein
    • Hughes, T. R., R. G. Weilbaecher, M. Walterscheid, and V. Lundblad. 2000. Identification of the single-strand telomeric DNA binding domain of the Saccharomyces cerevisiae Cdc13 protein. Proc. Natl. Acad. Sci. USA 97:6457-6462.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6457-6462
    • Hughes, T.R.1    Weilbaecher, R.G.2    Walterscheid, M.3    Lundblad, V.4
  • 26
    • 0032899753 scopus 로고    scopus 로고
    • Structure of a HAP1-DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein
    • King, D. A., L. Zhang, L. Guarente, and R. Marmorstein. 1999. Structure of a HAP1-DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein. Nat. Struct. Biol. 6:64-71.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 64-71
    • King, D.A.1    Zhang, L.2    Guarente, L.3    Marmorstein, R.4
  • 27
    • 0032862989 scopus 로고    scopus 로고
    • Cloning and characterisation of the chicken gene encoding the telomeric protein TRF2
    • Konrad, J. P., W. Mills, D. J. Easty, and C. J. Farr. 1999. Cloning and characterisation of the chicken gene encoding the telomeric protein TRF2. Gene 239:81-90.
    • (1999) Gene , vol.239 , pp. 81-90
    • Konrad, J.P.1    Mills, W.2    Easty, D.J.3    Farr, C.J.4
  • 29
    • 0037058877 scopus 로고    scopus 로고
    • Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe
    • Lei, M., P. Baumann, and T. R. Cech. 2002. Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe. Biochemistry 41:14560-14568.
    • (2002) Biochemistry , vol.41 , pp. 14560-14568
    • Lei, M.1    Baumann, P.2    Cech, T.R.3
  • 30
    • 0345304903 scopus 로고    scopus 로고
    • DNA self-recognition in the structure of Potl bound to telomeric single-stranded DNA
    • Lei, M., E. R. Podell, P. Baumann, and T. R. Cech. 2003. DNA self-recognition in the structure of Potl 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
  • 31
    • 1342293261 scopus 로고    scopus 로고
    • POT1 as a terminal transducer of TRF1 telomere length control
    • Loayza, D., and T. De Lange. 2003. POT1 as a terminal transducer of TRF1 telomere length control. Nature 25:25.
    • (2003) Nature , vol.25 , pp. 25
    • Loayza, D.1    De Lange, T.2
  • 32
    • 0035072260 scopus 로고    scopus 로고
    • Cdc13 subcomplexes regulate multiple telomere functions
    • Lustig, A. J. 2001. Cdc13 subcomplexes regulate multiple telomere functions. Nat. Struct. Biol. 8:297-299.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 297-299
    • Lustig, A.J.1
  • 35
    • 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
  • 36
    • 0036176232 scopus 로고    scopus 로고
    • Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA
    • Peersen, O. B., J. A. Ruggles, and S. C. Schultz. 2002. Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA. Nat. Struct. Biol. 9:182-187.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 182-187
    • Peersen, O.B.1    Ruggles, J.A.2    Schultz, S.C.3
  • 37
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • Pennock, E., K. Buckley, and V. Lundblad. 2001. Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell 104:387-396.
    • (2001) Cell , vol.104 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 39
    • 0026470324 scopus 로고
    • DNA recognition and binding by the Euplotes telomere protein
    • Price, C. M., R. Skopp, J. Krueger, and D. Williams. 1992. DNA recognition and binding by the Euplotes telomere protein. Biochemistry 31:10835-10843.
    • (1992) Biochemistry , vol.31 , pp. 10835-10843
    • Price, C.M.1    Skopp, R.2    Krueger, J.3    Williams, D.4
  • 40
    • 0037134452 scopus 로고    scopus 로고
    • The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)
    • Seimiya, H., and S. Smith. 2002. The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182). J. Biol. Chem. 277:14116-14126.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14116-14126
    • Seimiya, H.1    Smith, S.2
  • 41
    • 0036261517 scopus 로고    scopus 로고
    • Comparative mapping of human Chromosome 19 with the chicken shows conserved synteny and gives an insight into chromosomal evolution
    • Smith, J., I. R. Paton, F. Murray, R. P. Crooijmans, M. A. Groenen, and D. W. Burt. 2002. Comparative mapping of human Chromosome 19 with the chicken shows conserved synteny and gives an insight into chromosomal evolution. Mamm. Genome 13:310-315.
    • (2002) Mamm. Genome , vol.13 , pp. 310-315
    • Smith, J.1    Paton, I.R.2    Murray, F.3    Crooijmans, R.P.4    Groenen, M.A.5    Burt, D.W.6
  • 42
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly-(ADP-ribose) polymerase at human telomeres
    • Smith, S., I. Giriat, A. Schmitt, and T. de Lange. 1998. Tankyrase, a poly-(ADP-ribose) polymerase at human telomeres. Science 282:1484-1487.
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    De Lange, T.4
  • 43
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel, R. M., T. de Lange, and J. D. Griffith. 2001. T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang. EMBO J. 20:5532-5540.
    • (2001) EMBO J. , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    De Lange, T.2    Griffith, J.D.3
  • 44
    • 0344196810 scopus 로고    scopus 로고
    • The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes
    • Tan, M., C. Wei, and C. Price. 2003. The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Gene 323:1-10.
    • (2003) Gene , vol.323 , pp. 1-10
    • Tan, M.1    Wei, C.2    Price, C.3
  • 47
    • 0042035638 scopus 로고    scopus 로고
    • Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes
    • Theobald, D. L., and S. C. Schultz. 2003. Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes. EMBO J. 22:4314-4324.
    • (2003) EMBO J. , vol.22 , pp. 4314-4324
    • Theobald, D.L.1    Schultz, S.C.2
  • 48
    • 0032440892 scopus 로고    scopus 로고
    • Telomerase expression in chickens: Constitutive activity in somatic tissues and down-regulation in culture
    • Venkatesan, R. N., and C. Price. 1998. Telomerase expression in chickens: constitutive activity in somatic tissues and down-regulation in culture. Proc. Natl. Acad. Sci. USA 95:14763-14768.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14763-14768
    • Venkatesan, R.N.1    Price, C.2
  • 49
    • 0242349890 scopus 로고    scopus 로고
    • Protecting the terminus: T-loops and telomere end-binding proteins
    • Wei, C., and C. M. Price. 2003. Protecting the terminus: T-loops and telomere end-binding proteins. Cell. Mol. Life Sci. 60:2283-2294.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2283-2294
    • Wei, C.1    Price, C.M.2
  • 50
  • 52
    • 0342561644 scopus 로고    scopus 로고
    • Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres
    • Zhu, X. D., B. Kuster, M. Mann, J. H. Petrini, and T. Lange. 2000. Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat. Genet. 25:347-352.
    • (2000) Nat. Genet. , vol.25 , pp. 347-352
    • Zhu, X.D.1    Kuster, B.2    Mann, M.3    Petrini, J.H.4    Lange, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.