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Volumn 6, Issue 1, 2005, Pages 39-45

How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures

Author keywords

Telomeric DNA recognition; TRF1; TRF2; Water mediated contacts; X ray crystallography

Indexed keywords

DOUBLE STRANDED DNA; RAP PROTEIN; TELOMERE BINDING PROTEIN; TELOMERIC REPEAT BINDING FACTOR 1; TELOMERIC REPEAT BINDING FACTOR 2; DNA; HOMEODOMAIN PROTEIN; WATER;

EID: 21444444520     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400314     Document Type: Article
Times cited : (189)

References (42)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F-1 ATPase
    • Abrahams JP, Leslie ACW (1996) Methods used in the structure determination of bovine mitochondrial F-1 ATPase. Acta Crystallogr D 52: 30-42
    • (1996) Acta Crystallogr D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.C.W.2
  • 2
    • 0032211413 scopus 로고    scopus 로고
    • Role of the telomeric DNA-binding protein TRF2 in the stability of human chromosome ends
    • Ancelin K, Brun C, Gilson E (1998) Role of the telomeric DNA-binding protein TRF2 in the stability of human chromosome ends. BioEssays 20: 879-883
    • (1998) BioEssays , vol.20 , pp. 879-883
    • Ancelin, K.1    Brun, C.2    Gilson, E.3
  • 7
    • 84984775429 scopus 로고    scopus 로고
    • Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2
    • Broccoli D, Smogorzewska A, Chong L, de Lange T (1997) Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat Genet 17: 231-235
    • (1997) Nat Genet , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    De Lange, T.4
  • 8
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT et al (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54: 905-921
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 10
    • 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
  • 11
    • 1842683257 scopus 로고    scopus 로고
    • T-loops and the origin of telomeres
    • de Lange T (2004) T-loops and the origin of telomeres. Nat Rev Mol Cell Biol 5: 323-329
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 323-329
    • De Lange, T.1
  • 13
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall L, Chapman L, Moss H, de Lange T, Rhodes D (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
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M (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    Kjeldgaard, M.4
  • 16
  • 17
    • 0033605145 scopus 로고    scopus 로고
    • p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2
    • Karlseder J, Broccoli D, Dai Y, Hardy S, de Lange T (1999) p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2. Science 283: 1321-1325
    • (1999) Science , vol.283 , pp. 1321-1325
    • Karlseder, J.1    Broccoli, D.2    Dai, Y.3    Hardy, S.4    De Lange, T.5
  • 19
    • 0030498233 scopus 로고    scopus 로고
    • XdlMAPMAN and xdlDATAMAN-programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt GJ, Jones TA (1996) xdlMAPMAN and xdlDATAMAN-programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr D 52: 826-828
    • (1996) Acta Crystallogr D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 20
    • 0031081482 scopus 로고    scopus 로고
    • Recognition of telomeric DNA
    • Konig P, Rhodes D (1997) Recognition of telomeric DNA. Trends Biochem Sci 22: 43-47
    • (1997) Trends Biochem Sci , vol.22 , pp. 43-47
    • Konig, P.1    Rhodes, D.2
  • 21
    • 0029963828 scopus 로고    scopus 로고
    • The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA
    • Konig P, Giraldo R, Chapman L, Rhodes D (1996) The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. Cell 85: 125-136
    • (1996) Cell , vol.85 , pp. 125-136
    • Konig, P.1    Giraldo, R.2    Chapman, L.3    Rhodes, D.4
  • 22
    • 2642653129 scopus 로고    scopus 로고
    • Sequence-specific DNA recognition by the myb-like domain of the human telomere binding protein TRF1 : A model for the protein-DNA complex
    • Konig P, Fairall L, Rhodes D (1998) Sequence-specific DNA recognition by the myb-like domain of the human telomere binding protein TRF1 : a model for the protein-DNA complex. Nucleic Acids Res 26: 1731-1740
    • (1998) Nucleic Acids Res , vol.26 , pp. 1731-1740
    • Konig, P.1    Fairall, L.2    Rhodes, D.3
  • 23
    • 0003802953 scopus 로고    scopus 로고
    • Advances in MIR and MAD phasing: Maximum-likelihood refinement in a graphical environment, with SHARP
    • Wilson GDKS, Ashton AK, Bailey S (eds). Warrington, UK: Daresbury Laboratory
    • La Fortelle E, Irwin JJ, Bricogne G (1997) Advances in MIR and MAD phasing: maximum-likelihood refinement in a graphical environment, with SHARP. In Proceedings of the CCP4 Study Weekend, Wilson GDKS, Ashton AK, Bailey S (eds). Warrington, UK: Daresbury Laboratory
    • (1997) Proceedings of the CCP4 Study Weekend
    • La Fortelle, E.1    Irwin, J.J.2    Bricogne, G.3
  • 24
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: Conventions and principles
    • Lavery R, Sklenar H (1989) Defining the structure of irregular nucleic acids: conventions and principles. J Biomol Struct Dyn 6: 655-667
    • (1989) J Biomol Struct Dyn , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2
  • 25
    • 0028928198 scopus 로고
    • Conserved nucleoprotein structure at the ends of vertebrate and invertebrate chromosomes
    • Lejnine S, Makarov VL, Langmore JP (1995) Conserved nucleoprotein structure at the ends of vertebrate and invertebrate chromosomes. Proc Natl Acad Sci USA 92: 2393-2397
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2393-2397
    • Lejnine, S.1    Makarov, V.L.2    Langmore, J.P.3
  • 26
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie AGW (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newslett Protein Crystallogr, issue 26
    • (1992) Joint CCP4+ESF-EAMCB Newslett Protein Crystallogr , Issue.26
    • Leslie, A.G.W.1
  • 27
    • 0034716904 scopus 로고    scopus 로고
    • Identification of human Rap1 : Implications for telomere evolution
    • Li B, Oestreich S, de Lange T (2000) Identification 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
  • 29
    • 3342974395 scopus 로고    scopus 로고
    • Closed chromatin loops at the ends of chromosomes
    • Nikitina T, Woodcock CL (2004) Closed chromatin loops at the ends of chromosomes. J Cell Biol 166: 161-165
    • (2004) J Cell Biol , vol.166 , pp. 161-165
    • Nikitina, T.1    Woodcock, C.L.2
  • 30
    • 0032529088 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of human telomeric protein, hTRF1
    • Nishikawa T, Nagadoi A, Yoshimura S, Aimoto S, Nishimura Y (1998) Solution structure of the DNA-binding domain of human telomeric protein, hTRF1 Structure 6: 1057-1065
    • (1998) Structure , vol.6 , pp. 1057-1065
    • Nishikawa, T.1    Nagadoi, A.2    Yoshimura, S.3    Aimoto, S.4    Nishimura, Y.5
  • 32
    • 0026776412 scopus 로고
    • Solution structure of a DNA-binding unit of Myb: A helix-turn-helix- related motif with conserved tryptophans forming a hydrophobia core
    • Ogata K, Hojo H, Aimoto S, Nakai T, Nakamura H, Sarai A, Ishii S, Nishimura Y (1992) Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobia core. Proc Natl Acad Sci USA 89: 6428-6432
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6428-6432
    • Ogata, K.1    Hojo, H.2    Aimoto, S.3    Nakai, T.4    Nakamura, H.5    Sarai, A.6    Ishii, S.7    Nishimura, Y.8
  • 34
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosome core DNA
    • Satchwell SC, Drew HR, Travers AA (1986) Sequence periodicities in chicken nucleosome core DNA. J Mol Biol 191: 659-675
    • (1986) J Mol Biol , vol.191 , pp. 659-675
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 35
    • 2042429168 scopus 로고    scopus 로고
    • Regulation of telomerase by telomeric proteins
    • Smogorzewska A, De Lange T (2004) Regulation of telomerase by telomeric proteins. Annu Rev Biochem 73: 177-208
    • (2004) Annu Rev Biochem , vol.73 , pp. 177-208
    • Smogorzewska, A.1    De Lange, T.2
  • 37
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel RM, de Lange T, Griffith JD (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
  • 40
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel B, de Lange T (1997) Control of telomere length by the human telomeric protein TRF1. Nature 385: 740-743
    • (1997) Nature , vol.385 , pp. 740-743
    • Van Steensel, B.1    De Lange, T.2
  • 41
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel B, Smogorzewska A, de Lange T (1998) TRF2 protects human telomeres from end-to-end fusions. Cell 92: 401-413
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 42


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.