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Volumn 6, Issue , 2016, Pages

Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MULTIPROTEIN COMPLEX; TELOMERIC REPEAT BINDING FACTOR 2; TERF2 PROTEIN, HUMAN;

EID: 84957585065     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep20513     Document Type: Article
Times cited : (28)

References (60)
  • 1
    • 84871749525 scopus 로고    scopus 로고
    • Mechanisms of telomere loss and their consequences for chromosome instability
    • Muraki, K., Nyhan, K., Han, L. & Murnane, J. P. Mechanisms of telomere loss and their consequences for chromosome instability. Front Oncol 2, 135 (2012).
    • (2012) Front Oncol , vol.2 , pp. 135
    • Muraki, K.1    Nyhan, K.2    Han, L.3    Murnane, J.P.4
  • 2
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • Palm, W. & de Lange, T. How shelterin protects mammalian telomeres. Annu Rev Genet 42, 301-34 (2008).
    • (2008) Annu Rev Genet , vol.42 , pp. 301-334
    • Palm, W.1    De Lange, T.2
  • 5
    • 48549086606 scopus 로고    scopus 로고
    • Ulcerative colitis is a disease of accelerated colon aging: Evidence from telomere attrition and DNA damage
    • Risques, R. A. et al. Ulcerative colitis is a disease of accelerated colon aging: evidence from telomere attrition and DNA damage. Gastroenterology 135, 410-8 (2008).
    • (2008) Gastroenterology , vol.135 , pp. 410-418
    • Risques, R.A.1
  • 8
    • 84900443034 scopus 로고    scopus 로고
    • Cell biology of disease: Telomeropathies: An emerging spectrum disorder
    • Holohan, B., Wright, W. E. & Shay, J. W. Cell biology of disease: Telomeropathies: an emerging spectrum disorder. J Cell Biol 205, 289-99 (2014).
    • (2014) J Cell Biol , vol.205 , pp. 289-299
    • Holohan, B.1    Wright, W.E.2    Shay, J.W.3
  • 9
    • 0030731928 scopus 로고    scopus 로고
    • Normal human chromosomes have long G-rich telomeric overhangs at one end
    • Wright, W. E., Tesmer, V. M., Huffman, K. E., Levene, S. D. & Shay, J. W. Normal human chromosomes have long G-rich telomeric overhangs at one end. Genes Dev 11, 2801-9 (1997).
    • (1997) Genes Dev , vol.11 , pp. 2801-2809
    • Wright, W.E.1    Tesmer, V.M.2    Huffman, K.E.3    Levene, S.D.4    Shay, J.W.5
  • 10
    • 0842346436 scopus 로고    scopus 로고
    • Beginning to understand the end of the chromosome
    • Cech, T. R. Beginning to understand the end of the chromosome. Cell 116, 273-9 (2004).
    • (2004) Cell , vol.116 , pp. 273-279
    • Cech, T.R.1
  • 11
    • 33745046135 scopus 로고    scopus 로고
    • Inside the mammalian telomere interactome: Regulation and regulatory activities of telomeres
    • Songyang, Z. & Liu, D. Inside the mammalian telomere interactome: regulation and regulatory activities of telomeres. Crit Rev Eukaryot Gene Expr 16, 103-18 (2006).
    • (2006) Crit Rev Eukaryot Gene Expr , vol.16 , pp. 103-118
    • Songyang, Z.1    Liu, D.2
  • 12
    • 34250841785 scopus 로고    scopus 로고
    • Replication and protection of telomeres
    • Verdun, R. E. & Karlseder, J. Replication and protection of telomeres. Nature 447, 924-31 (2007).
    • (2007) Nature , vol.447 , pp. 924-931
    • Verdun, R.E.1    Karlseder, J.2
  • 13
    • 11144223025 scopus 로고    scopus 로고
    • Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities
    • Hanaoka, S., Nagadoi, A. & Nishimura, Y. Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities. Protein Sci 14, 119-30 (2005).
    • (2005) Protein Sci , vol.14 , pp. 119-130
    • Hanaoka, S.1    Nagadoi, A.2    Nishimura, Y.3
  • 14
    • 0033553536 scopus 로고    scopus 로고
    • Mammalian telomeres end in a large duplex loop
    • Griffith, J. D. et al. Mammalian telomeres end in a large duplex loop. Cell 97, 503-14 (1999).
    • (1999) Cell , vol.97 , pp. 503-514
    • Griffith, J.D.1
  • 15
    • 0033406877 scopus 로고    scopus 로고
    • Telomeres of polytene chromosomes in a ciliated protozoan terminate in duplex DNA loops
    • Murti, K. G. & Prescott, D. M. Telomeres of polytene chromosomes in a ciliated protozoan terminate in duplex DNA loops. Proc Natl Acad Sci USA 96, 14436-9 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14436-14439
    • Murti, K.G.1    Prescott, D.M.2
  • 18
    • 1842683257 scopus 로고    scopus 로고
    • T-loops and the origin of telomeres
    • de Lange, T. T-loops and the origin of telomeres. Nat Rev Mol Cell Biol 5, 323-9 (2004).
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 323-329
    • De Lange, T.1
  • 19
    • 84885580087 scopus 로고    scopus 로고
    • Super-Resolution Fluorescence Imaging of Telomeres Reveals TRF2-Dependent T-loop Formation
    • Doksani, Y., Wu, J. Y., de Lange, T. & Zhuang, X. Super-Resolution Fluorescence Imaging of Telomeres Reveals TRF2-Dependent T-loop Formation. Cell 155, 345-56 (2013).
    • (2013) Cell , vol.155 , pp. 345-356
    • Doksani, Y.1    Wu, J.Y.2    De Lange, T.3    Zhuang, X.4
  • 20
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel, B., Smogorzewska, A. & de Lange, T. TRF2 protects human telomeres from end-to-end fusions. Cell 92, 401-13 (1998).
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 21
    • 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. p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2. Science 283, 1321-5 (1999).
    • (1999) Science , vol.283 , pp. 1321-1325
    • Karlseder, J.1    Broccoli, D.2    Dai, Y.3    Hardy, S.4    De Lange, T.5
  • 23
    • 33846969882 scopus 로고    scopus 로고
    • A topological mechanism for TRF2-enhanced strand invasion
    • Amiard, S. et al. A topological mechanism for TRF2-enhanced strand invasion. Nat Struct Mol Biol 14, 147-54 (2007).
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 147-154
    • Amiard, S.1
  • 24
    • 0032562649 scopus 로고    scopus 로고
    • TRF1 promotes parallel pairing of telomeric tracts in vitro
    • Griffith, J., Bianchi, A. & de Lange, T. TRF1 promotes parallel pairing of telomeric tracts in vitro. J Mol Biol 278, 79-88 (1998).
    • (1998) J Mol Biol , vol.278 , pp. 79-88
    • Griffith, J.1    Bianchi, A.2    De Lange, T.3
  • 25
    • 0036712485 scopus 로고    scopus 로고
    • Dynamic atomic force microscopy methods
    • Garcia, R. & Perez, R. Dynamic atomic force microscopy methods. Surface Science Reports 47, 197-301 (2002).
    • (2002) Surface Science Reports , vol.47 , pp. 197-301
    • Garcia, R.1    Perez, R.2
  • 26
    • 0037328523 scopus 로고    scopus 로고
    • Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy
    • Yang, Y., Wang, H. & Erie, D. A. Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy. Methods 29, 175-87 (2003).
    • (2003) Methods , vol.29 , pp. 175-187
    • Yang, Y.1    Wang, H.2    Erie, D.A.3
  • 28
    • 34948833721 scopus 로고    scopus 로고
    • Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy
    • Sinensky, A. K. & Belcher, A. M. Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy. Nat Nanotechnol 2, 653-9 (2007).
    • (2007) Nat Nanotechnol , vol.2 , pp. 653-659
    • Sinensky, A.K.1    Belcher, A.M.2
  • 29
    • 28844431517 scopus 로고    scopus 로고
    • Scanning Kelvin nanoprobe detection in materials science and biochemical analysis
    • Cheran, L. E., Sadeghi, S. & Thompson, M. Scanning Kelvin nanoprobe detection in materials science and biochemical analysis. Analyst 130, 1569-76 (2005).
    • (2005) Analyst , vol.130 , pp. 1569-1576
    • Cheran, L.E.1    Sadeghi, S.2    Thompson, M.3
  • 30
    • 11144239969 scopus 로고    scopus 로고
    • Label-free detection of nucleic acid and protein microarrays by scanning Kelvin nanoprobe
    • Thompson, M. et al. Label-free detection of nucleic acid and protein microarrays by scanning Kelvin nanoprobe. Biosens Bioelectron 20, 1471-81 (2005).
    • (2005) Biosens Bioelectron , vol.20 , pp. 1471-1481
    • Thompson, M.1
  • 31
    • 65149101444 scopus 로고    scopus 로고
    • Electrostatic force microscopy: Imaging DNA and protein polarizations one by one
    • Mikamo-Satoh, E., Yamada, F., Takagi, A., Matsumoto, T. & Kawai, T. Electrostatic force microscopy: imaging DNA and protein polarizations one by one. Nanotechnology 20, 145102 (2009).
    • (2009) Nanotechnology , vol.20
    • Mikamo-Satoh, E.1    Yamada, F.2    Takagi, A.3    Matsumoto, T.4    Kawai, T.5
  • 32
    • 84957441357 scopus 로고    scopus 로고
    • Visualizing the Path of DNA through Proteins using DREEM Imaging
    • Wu, D. et al. Visualizing the Path of DNA through Proteins using DREEM Imaging. Mol Cell 61(2), 315-323 (2016).
    • (2016) Mol Cell , vol.61 , Issue.2 , pp. 315-323
    • Wu, D.1
  • 33
    • 79953202369 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions using atomic force microscopy
    • ed. Schuck, P. Springer Science + Business Media, LLC
    • Wang, H., Yang, Y. & Erie, D. A. Characterization of protein-protein interactions using atomic force microscopy in Protein Interactions Biophysical approaches for the study of complex reversible systems, Vol. 5 (ed. Schuck, P.) 39-78 (Springer Science + Business Media, LLC, 2007).
    • (2007) Protein Interactions Biophysical Approaches for the Study of Complex Reversible Systems , vol.5 , pp. 39-78
    • Wang, H.1    Yang, Y.2    Erie, D.A.3
  • 34
    • 0029866788 scopus 로고    scopus 로고
    • Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids
    • Hansma, H. G., Revenko, I., Kim, K. & Laney, D. E. Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids. Nucleic Acids Res 24, 713-20 (1996).
    • (1996) Nucleic Acids Res , vol.24 , pp. 713-720
    • Hansma, H.G.1    Revenko, I.2    Kim, K.3    Laney, D.E.4
  • 35
    • 84859340760 scopus 로고    scopus 로고
    • The N-terminal domains of TRF1 and TRF2 regulate their ability to condense telomeric DNA
    • Poulet, A. et al. The N-terminal domains of TRF1 and TRF2 regulate their ability to condense telomeric DNA. Nucleic Acids Res 40, 2566-76 (2012).
    • (2012) Nucleic Acids Res , vol.40 , pp. 2566-2576
    • Poulet, A.1
  • 36
    • 33847026837 scopus 로고    scopus 로고
    • Using atomic force microscopy to study chromatin structure and nucleosome remodeling
    • Lohr, D., Bash, R., Wang, H., Yodh, J. & Lindsay, S. Using atomic force microscopy to study chromatin structure and nucleosome remodeling. Methods 41, 333-41 (2007).
    • (2007) Methods , vol.41 , pp. 333-341
    • Lohr, D.1    Bash, R.2    Wang, H.3    Yodh, J.4    Lindsay, S.5
  • 37
    • 84907320786 scopus 로고    scopus 로고
    • Solution-state conformation and stoichiometry of yeast Sir3 heterochromatin fibres
    • Swygert, S. G. et al. Solution-state conformation and stoichiometry of yeast Sir3 heterochromatin fibres. Nat Commun 5, 4751 (2014).
    • (2014) Nat Commun , vol.5 , pp. 4751
    • Swygert, S.G.1
  • 38
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-60 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 39
    • 84862732690 scopus 로고    scopus 로고
    • New insights into nucleosome and chromatin structure: An ordered state or a disordered affair?
    • Luger, K., Dechassa, M. L. & Tremethick, D. J. New insights into nucleosome and chromatin structure: an ordered state or a disordered affair? Nat Rev Mol Cell Biol 13, 436-47 (2012).
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 436-447
    • Luger, K.1    Dechassa, M.L.2    Tremethick, D.J.3
  • 40
    • 84904717597 scopus 로고    scopus 로고
    • Single molecule studies of DNA mismatch repair
    • Erie, D. A. & Weninger, K. R. Single molecule studies of DNA mismatch repair. DNA Repair (Amst) 20, 71-81 (2014).
    • (2014) DNA Repair (Amst) , vol.20 , pp. 71-81
    • Erie, D.A.1    Weninger, K.R.2
  • 41
    • 41249087856 scopus 로고    scopus 로고
    • General purpose molecular dynamics simulations fully implemented on graphics processing units
    • Anderson, J. A., Lorenz, C. D. & Travesset, A. General purpose molecular dynamics simulations fully implemented on graphics processing units. Journal of Computational Physics 227, 28 (2008).
    • (2008) Journal of Computational Physics , vol.227 , pp. 28
    • Anderson, J.A.1    Lorenz, C.D.2    Travesset, A.3
  • 42
    • 84901820972 scopus 로고    scopus 로고
    • How molecular knots can pass through each other
    • Trefz, B., Siebert, J. & Virnau, P. How molecular knots can pass through each other. Proc Natl Acad Sci USA 111, 7948-51 (2014).
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 7948-7951
    • Trefz, B.1    Siebert, J.2    Virnau, P.3
  • 43
    • 84895821906 scopus 로고    scopus 로고
    • TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres
    • Lin, J. et al. TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres. Nucleic Acids Res 42, 2493-504 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. 2493-2504
    • Lin, J.1
  • 44
    • 84884333270 scopus 로고    scopus 로고
    • Nonspecific bridging-induced attraction drives clustering of DNA-binding proteins and genome organization
    • Brackley, C. A., Taylor, S., Papantonis, A., Cook, P. R. & Marenduzzo, D. Nonspecific bridging-induced attraction drives clustering of DNA-binding proteins and genome organization. Proc Natl Acad Sci USA 110, E3605-11 (2013).
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E3605-E3611
    • Brackley, C.A.1    Taylor, S.2    Papantonis, A.3    Cook, P.R.4    Marenduzzo, D.5
  • 45
    • 84957428149 scopus 로고    scopus 로고
    • TRF2-Mediated Control of Telomere DNA Topology as a Mechanism for Chromosome-End Protection
    • Benarroch-Popivker, D. et al. TRF2-Mediated Control of Telomere DNA Topology as a Mechanism for Chromosome-End Protection. Mol Cell 61(2), 274-286 (2016).
    • (2016) Mol Cell , vol.61 , Issue.2 , pp. 274-286
    • Benarroch-Popivker, D.1
  • 46
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel, R. M., de Lange, T. & Griffith, J. D. T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang. Embo J 20, 5532-40 (2001).
    • (2001) Embo J , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    De Lange, T.2    Griffith, J.D.3
  • 47
    • 84860854071 scopus 로고    scopus 로고
    • RTEL1 dismantles T loops and counteracts telomeric G4-DNA to maintain telomere integrity
    • Vannier, J. B., Pavicic-Kaltenbrunner, V., Petalcorin, M. I., Ding, H. & Boulton, S. J. RTEL1 dismantles T loops and counteracts telomeric G4-DNA to maintain telomere integrity. Cell 149, 795-806 (2012).
    • (2012) Cell , vol.149 , pp. 795-806
    • Vannier, J.B.1    Pavicic-Kaltenbrunner, V.2    Petalcorin, M.I.3    Ding, H.4    Boulton, S.J.5
  • 49
    • 0037175018 scopus 로고    scopus 로고
    • Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases
    • Opresko, P. L. et al. Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J Biol Chem 277, 41110-9 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 41110-41119
    • Opresko, P.L.1
  • 50
    • 77955070324 scopus 로고    scopus 로고
    • Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase
    • Nora, G. J., Buncher, N. A. & Opresko, P. L. Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase. Nucleic Acids Res 38, 3984-98 (2010).
    • (2010) Nucleic Acids Res , vol.38 , pp. 3984-3998
    • Nora, G.J.1    Buncher, N.A.2    Opresko, P.L.3
  • 51
    • 84858976265 scopus 로고    scopus 로고
    • Biochemical analysis of the human mismatch repair proteins hMutSalpha MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D)
    • Geng, H. et al. Biochemical analysis of the human mismatch repair proteins hMutSalpha MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D). J Biol Chem 287, 9777-91 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 9777-9791
    • Geng, H.1
  • 52
    • 0028557213 scopus 로고
    • Stringent sequence requirements for the formation of human telomeres
    • Hanish, J. P., Yanowitz, J. L. & de Lange, T. Stringent sequence requirements for the formation of human telomeres. Proc Natl Acad Sci USA 91, 8861-5 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8861-8865
    • Hanish, J.P.1    Yanowitz, J.L.2    De Lange, T.3
  • 53
    • 79955466020 scopus 로고    scopus 로고
    • In vitro studies of DNA mismatch repair proteins
    • Geng, H. et al. In vitro studies of DNA mismatch repair proteins. Anal Biochem 413, 179-84 (2011).
    • (2011) Anal Biochem , vol.413 , pp. 179-184
    • Geng, H.1
  • 54
    • 78651249446 scopus 로고    scopus 로고
    • Antibody-unfolding and metastable-state binding in force spectroscopy and recognition imaging
    • Kaur, P. et al. Antibody-unfolding and metastable-state binding in force spectroscopy and recognition imaging. Biophys J 100, 243-50 (2011).
    • (2011) Biophys J , vol.100 , pp. 243-250
    • Kaur, P.1
  • 56
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials
    • Shlyakhtenko, L. S. et al. Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials. Ultramicroscopy 97, 279-87 (2003).
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.S.1
  • 57
    • 33845987076 scopus 로고    scopus 로고
    • The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats
    • Fouche, N. et al. The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats. J Biol Chem 281, 37486-95 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 37486-37495
    • Fouche, N.1
  • 58
    • 62649104650 scopus 로고    scopus 로고
    • TRF2 promotes, remodels and protects telomeric Holliday junctions
    • Poulet, A. et al. TRF2 promotes, remodels and protects telomeric Holliday junctions. EMBO J 28, 641-51 (2009).
    • (2009) EMBO J , vol.28 , pp. 641-651
    • Poulet, A.1
  • 59
    • 48449096251 scopus 로고    scopus 로고
    • Ionic effects on the equilibrium dynamics of DNA confined in nanoslits
    • Hsieh, C. C., Balducci, A. & Doyle, P. S. Ionic effects on the equilibrium dynamics of DNA confined in nanoslits. Nano Letters 8, 1683-1688 (2008).
    • (2008) Nano Letters , vol.8 , pp. 1683-1688
    • Hsieh, C.C.1    Balducci, A.2    Doyle, P.S.3


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