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The epigenetic regulation of mammalian telomeres

Blasco, María A.·2007·Nature Reviews Genetics

Abstract

Increasing evidence indicates that chromatin modifications are important regulators of mammalian telomeres. Telomeres provide well studied paradigms of heterochromatin formation in yeast and flies, and recent studies have shown that mammalian telomeres and subtelomeric regions are also enriched in epigenetic marks that are characteristic of heterochromatin. Furthermore, the abrogation of master epigenetic regulators, such as histone methyltransferases and DNA methyltransferases, correlates with loss of telomere-length control, and telomere shortening to a critical length affects the epigenetic status of telomeres and subtelomeres. These links between epigenetic status and telomere-length regulation provide important new avenues for understanding processes such as cancer development and ageing, which are characterized by telomere-length defects.

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  • Loss of heterochromatic marks at telomeres leads to telomere lengthening.

    “Of note, loss of heterochromatic marks at telomeres has been shown to lead to telomere lengthening 54 .”

    From Hallmarks of aging: An expanding universe (2023) · cites this paper as [54]

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  1. Chan, S. W. & Blackburn, E. H. New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin. Oncogene 21, 553–563 (2002). · DOI
  2. Liu, D., O'Connor, M. S., Qin, J. & Songyang, Z. Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279, 51338–51342 (2004). · DOI · Paper page
  3. Collins, K. & Mitchell, J. R. Telomerase in the human organism. Oncogene 21, 564–579 (2002). · DOI
  4. Muntoni, A. & Reddel, R. R. The first molecular details of ALT in human tumor cells. Hum. Mol. Genet. 14, 191–196 (2005). · DOI
  5. Dunham, M. A., Neumann, A. A., Fasching, C. L. & Reddel, R. R. Telomere maintenance by recombination in human cells. Nature Genet. 26, 447–450 (2000). · DOI · Paper page
  6. Slagboom, P. E., Droog, S. & Boomsma, D. I. Genetic determination of telomere size in humans: a twin study of three age groups. Am. J. Hum. Genet. 55, 876–882 (1994).
  7. Zhu, L. et al. Telomere length regulation in mice is linked to a novel chromosome locus. Proc. Natl Acad. Sci. USA 95, 8648–8653 (1998). · DOI
  8. Flores, I., Cayuela, M. L. & Blasco, M. A. Effects of telomerase and telomere length on epidermal stem cell behavior. Science 309, 1253–1256 (2005). · DOI · Paper page
  9. Shay, J. W. & Wright, W. E. Telomerase therapeutics for cancer: challenges and new directions. Nature Rev. Drug Discov. 5, 577–584 (2006). · DOI
  10. Baur, J. A., Zou, Y., Shay, J. W. & Wright, W. E. Telomere position effect in human cells. Science 292, 2075 (2001). · DOI
  11. Koering, C. E. et al. Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity. EMBO Rep. 3, 1055–1061 (2002). References 15 and 16 provide conclusive evidence that TPE (or 'silencing' of genes near the telomeres) operates in mammalian cells. · DOI
  12. Makarov, V. L., Lejnine, S., Bedoyan, J. & Langmore, J. P. Nucleosomal organization of telomere-specific chromatin in rat. Cell 73, 775–787 (1993). · DOI
  13. Tommerup, H., Dousmanis, A. & de Lange, T. Unusual chromatin in human telomeres. Mol. Cell. Biol. 14, 5777–5785 (1994). · DOI
  14. Garcia-Cao, M., O'Sullivan, R., Peters, A. H., Jenuwein, T. & Blasco, M. A. Epigenetic regulation of telomere length in mammalian cells by the SUV39H1 and SUV39H2 histone methyltransferases. Nature Genet. 36, 94–99 (2004). · DOI
  15. Gonzalo, S. et al. DNA methyltransferases control telomere length and telomere recombination in mammalian cells. Nature Cell Biol. 8, 416–424 (2006). This work shows that mammalian subtelomeric DNA is heavily methylated, and that this epigenetic modification acts as a negative regulator of telomere length and telomere recombination independently of histone methylation. · DOI · Paper page
  16. Fraga, M. F. et al. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nature Genet. 37, 391–400 (2005). · DOI
  17. van Overveld, P. G. et al. Hypomethylation of D4Z4 in 4q-linked and non-4q-linked facioscapulohumeral muscular dystrophy. Nature Genet. 35, 315–317 (2003). · DOI
  18. Blasco, M. A. Telomeres and human disease: ageing, cancer and beyond. Nature Rev. Genet. 6, 611–622 (2005). · DOI · Paper page
  19. Griffith, J. D. et al. Mammalian telomeres end in a large duplex loop. Cell 97, 503–514 (1999). · DOI · Paper page
  20. Conrad, M. N., Wright, J. H., Wolf, A. J. & Zakian, V. A. Rap1 protein interacts with yeast telomeres in vivo: overproduction alters telomere structure and decreases chromosome stability. Cell 63, 739–750 (1990). · DOI
  21. Nugent, C. I., Hughes, T. R., Lue, N. F. & Lundblad, V. Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance. Science 274, 249–252 (1996). · DOI
  22. Tham, W. H. & Zakian, V. A. Transcriptional silencing at Saccharomyces telomeres: implications for other organisms. Oncogene 21, 512–521 (2002). A must-read review on budding yeast telomeric heterochromatin and its roles in controlling telomere length and telomeric silencing. · DOI
  23. Kyrion, G., Boakye, K. A. & Lustig, A. J. C-terminal truncation of RAP1 results in the deregulation of telomere size, stability, and function in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 5159–5173 (1992). · DOI
  24. Krauskopf, A. & Blackburn, E. H. Control of telomere growth by interactions of RAP1 with the most distal telomeric repeats. Nature 383, 354–357 (1996). · DOI
  25. Levy, D. L. & Blackburn, E. H. Counting of Rif1p and Rif2p on Saccharomyces cerevisiae telomeres regulates telomere length. Mol. Cell. Biol. 24, 10857–10867 (2004). · DOI
  26. Palladino, F. et al. SIR3 and SIR4 proteins are required for the positioning and integrity of yeast telomeres. Cell 75, 543–555 (1993). · DOI
  27. Cooper, J. P., Nimmo, E. R., Allshire, R. C. & Cech, T. R. Regulation of telomere length and function by a MYB-domain protein in fission yeast. Nature 385, 744–747 (1997). · DOI
  28. Baumann, P. & Cech, T. R. POT1, the putative telomere end-binding protein in fission yeast and humans. Science 292, 1171–1175 (2001). · DOI · Paper page
  29. Kanoh, J. & Ishikawa, F. spRap1 and spRif1, recruited to telomeres by Taz1, are essential for telomere function in fission yeast. Curr. Biol. 11, 1624–1630 (2001). · DOI
  30. Smith, S., Giriat, I., Schmitt, A. & de Lange, T. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282, 1484–1487 (1998). · DOI
  31. Hockemeyer, D., Daniela, J. P., Takai, H. & de Lange, T. Recent expansion of the telomeric complex in rodents: two distinct POT1 proteins protect mouse telomeres. Cell 126, 63–77 (2006). · DOI · Paper page
  32. Zhu, X. D., Kuster, B., Mann, M., Petrini, J. H. & Lange, T. Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nature Genet. 25, 347–352 (2000). · DOI
  33. Samper, E., Goytisolo, F. A., Slijepcevic, P., van Buul, P. P. & Blasco, M. A. Mammalian KU86 protein prevents telomeric fusions independently of the length of TTAGGG repeats and the G-strand overhang. EMBO Rep. 1, 244–252 (2000). · DOI
  34. Tarsounas, M. et al. Telomere maintenance requires the RAD51D recombination/repair protein. Cell 117, 337–347 (2004). · DOI
  35. Karlseder, J. et al. The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response. PLoS Biol. 2, e240 (2004). · DOI
  36. Bradshaw, P. S., Stavropoulos, D. J & Meyn, M. S. Human telomeric protein TRF2 associates with genomic double-strand breaks as an early response to DNA damage. Nature Genet. 37, 193–197 (2005). · DOI
  37. Oh, B.-K., Kim, Y.-J., Park, C. & Park, Y. N. Up-regulation of telomere-binding proteins, TRF1, TRF2, and TIN2 is related to telomere shortening during human multistep hepatocarcinogenesis. Am. J. Pathol. 166, 73–80 (2005). · DOI
  38. Matsutani, N. et al. Expression of telomeric repeat binding factor 1 and 2 and TRF1-interacting nuclear protein 2 in human gastric carcinomas. Int. J. Oncol. 19, 507–512 (2001).
  39. Muñoz, P. et al. XPF nuclease-dependent telomere loss and increased DNA damage in mice overexpressing TRF2 result in premature aging and cancer. Nature Genet. 10, 1063 (2005). · DOI
  40. Nakanishi, K. et al. Expression of mRNAs for telomeric repeat binding factor (TRF)-1 and TRF2 in atypical adenomatous hyperplasia and adenocarcinoma of the lung. Clin. Cancer Res. 9, 1105–1111 (2003).
  41. Bellon, M. et al. Increased expression of telomere length regulating factors TRF1, TRF2 and TIN2 in patients with adult T-cell leukemia. Int. J. Cancer 119, 2090–2097 (2006). · DOI
  42. Lazzerini Denchi, E., Celli, G. & de Lange, T. Hepatocytes with extensive telomere deprotection and fusion remain viable and regenerate liver mass through endoreduplication. Genes Dev. 20, 2648–2653 (2006). · DOI · Paper page
  43. Flores, I., Cayuela, M. L. & Blasco, M. A. Effects of telomerase and telomere length on epidermal stem cell behavior. Science 309, 1253–1256 (2005). · DOI · Paper page
  44. Mason, J. M. & Biessmann, H. The unusual telomeres of Drosophila. Trends Genet. 11, 58–62 (1995). · DOI
  45. Lundblad, V. & Blackburn, E. H. An alternative pathway for yeast telomere maintenance rescues est1- senescence. Cell 73, 347–360 (1993). · DOI · Paper page
  46. Lundblad, V. Telomere maintenance without telomerase. Oncogene 21, 522–531 (2002). · DOI
  47. Le, S., Moore, J. K., Haber, J. E. & Greider, C. W. RAD50 and RAD51 define two pathways that collaborate to maintain telomeres in the absence of telomerase. Genetics 152, 143–152 (1999). · DOI
  48. Teng, S. C. & Zakian, V. A. Telomere–telomere recombination is an efficient bypass pathway for telomere maintenance in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 8083–8093 (1999). · DOI
  49. Niida, H. et al. Telomere maintenance in telomerase-deficient mouse embryonic stem cells: characterization of an amplified telomeric DNA. Mol. Cell. Biol. 20, 4115–4127 (2000). · DOI
  50. Levis, R., Hazelrigg, T. & Rubin, G. M. Effects of genomic position on the expression of transduced copies of the white gene of Drosophila. Science 229, 558–561 (1985). · DOI
  51. Gottschling, D. E., Aparicio, O. M., Billington, B. L. & Zakian, V. A. Position effect at S. cerevisiae telomeres: reversible repression of Pol II transcription. Cell 63, 751–762 (1990). · DOI
  52. Nimmo, E. R., Cranston, G. & Allshire, R. C. Telomere-associated chromosome breakage in fission yeast results in variegated expression of adjacent genes. EMBO J. 13, 3801–3811 (1994). · DOI
  53. Kyrion, G., Liu, K., Liu, C. & Lustig, A. J. RAP1 and telomere structure regulate telomere position effects in Saccharomyces cerevisiae. Genes Dev. 7, 1146–1159 (1993). · DOI
  54. Aparicio, O. M., Billington, B. L. & Gottschling, D. E. Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66, 1279–1287 (1991). · DOI
  55. Hecht, A., Laroche, T., Strahl-Bolsinger, S., Gasser, S. M. & Grunstein, M. Histone H3 and H4 N-termini interact with Sir3 and Sir4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 80, 583–592 (1995). A molecular model for how heterochromatin is formed at budding yeast telomeres is first proposed here. · DOI
  56. Moretti, P. & Shore, D. Multiple interactions in Sir protein recruitment by Rap1p at silencers and telomeres in yeast. Mol. Cell. Biol. 21, 8082–8094 (2001). · DOI
  57. Wright, J. H., Gottschling, D. E. & Zakian, V. A. Saccharomyces telomeres assume a non-nucleosomal chromatin structure. Genes Dev. 6, 197–210 (1992). · DOI
  58. Luo, K., Vega-Palas, M. A. & Grunstein, M. Rap1–Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast. Genes Dev. 16, 1528–1539 (2002). · DOI
  59. Strahl-Bolsinger, S., Hecht, A., Luo, K. & Grunstein, M. SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev. 11, 83–93 (1997). · DOI
  60. de Bruin, D., Kantrow, S. M., Liberatore, R. A. & Zakian, V. A. Telomere folding is required for the stable maintenance of telomere position effects in yeast. Mol. Cell. Biol. 20, 7991–8000 (2000). · DOI
  61. Maillet, L. et al. Evidence for silencing compartments within the yeast nucleus: a role for telomere proximity and Sir protein concentration in silencer-mediated repression. Genes Dev. 10, 1796–1811 (1996). · DOI
  62. Fourel, G., Revardel, E., Koering, C. E. & Gilson, E. Cohabitation of insulators and silencing elements in yeast subtelomeric regions. EMBO J. 18, 2522–2537 (1999). · DOI
  63. Pryde, F. E. & Louism, E. J. Limitations of silencing at native yeast telomeres. EMBO J. 18, 2538–2550 (1999). · DOI
  64. Emre, N. C. et al. Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing. Mol. Cell 17, 585–594 (2005). · DOI
  65. Cenci, G. et al. UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior. Genes Dev. 11, 863–875 (1997). · DOI
  66. Greenwell, P. W. et al. TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene. Cell 82, 823–829 (1995). · DOI
  67. Porter, S. E., Greenwell, P. W., Ritchie, K. B. & Petes, T. D. The DNA-binding protein Hdf1p (a putative Ku homologue) is required for maintaining normal telomere length in Saccharomyces cerevisiae. Nucleic Acids Res. 24, 582–585 (1996). · DOI
  68. Nislow, C., Ray, E. & Pillus, L. SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes. Mol. Biol. Cell 8, 2421–2436 (1997). · DOI
  69. Gartenberg, M. R., Neumann, F. R., Laroche, T., Blaszczyk, M. & Gasser, S. M. Sir-mediated repression can occur independently of chromosomal and subnuclear contexts. Cell 119, 955–967 (2004). · DOI
  70. Berthiau, A. S. et al. Subtelomeric proteins negatively regulate telomere elongation in budding yeast. EMBO J. 25, 846–856 (2006). · DOI
  71. Hediger, F., Berthiau, A. S., van Houwe, G., Gilson, E. & Gasser, S. M. Subtelomeric factors antagonize telomere anchoring and Tel1-independent telomere length regulation. EMBO J. 25, 857–867 (2006). · DOI
  72. Teng, S. C., Chang, J., McCowan, B. & Zakian, V. A. Telomerase-independent lengthening of yeast telomeres occurs by an abrupt Rad50p-dependent, Rif-inhibited recombinational process. Mol. Cell 6, 947–952 (2000). · DOI
  73. Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D. & Grewal, S. I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110–113 (2001). · DOI · Paper page
  74. Volpe, T. A. et al. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 297, 1833–1837 (2002). · DOI
  75. Kanoh, J., Sadaie, M., Urano, T. & Ishikawa, F. Telomere binding protein Taz1 establishes Swi6 heterochromatin independently of RNAi at telomeres. Curr. Biol. 15, 1808–1819 (2005). · DOI
  76. Ueno, M. et al. Fission yeast Arp6 is required for telomere silencing, but functions independently of Swi6. Nucleic Acids Res. 32, 736–741 (2004). · DOI
  77. Ekwall, K. et al. Mutations in the fission yeast silencing factors clr4+ and rik1+ disrupt the localisation of the chromo domain protein Swi6p and impair centromere function. J. Cell Sci. 109, 2637–2648 (1996). · DOI
  78. Hall, I. M., Noma, K. & Grewal, S. I. RNA interference machinery regulates chromosome dynamics during mitosis and meiosis in fission yeast. Proc. Natl Acad. Sci. USA 100, 193–198 (2003). · DOI
  79. Perrini, B. et al. HP1 controls telomere capping, telomere elongation, and telomere silencing by two different mechanisms in Drosophila. Mol. Cell 15, 467–476 (2004). · DOI
  80. Savitsky, M., Kwon, D., Georgiev, P., Kalmykova, A. & Gvozdev, V. Telomere elongation is under the control of the RNAi-based mechanism in the Drosophila germline. Genes Dev. 20, 345–354 (2006). · DOI
  81. Xhemalce, B., Seeler, J. S., Thon, G., Dejean, A. & Arcangioli, B. Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. EMBO J. 23, 3844–3853 (2004). · DOI
  82. Xhemalce, B. et al. Role of SUMO in the dynamics of telomere maintenance in fission yeast. Proc. Natl Acad. Sci. USA. 104, 893–898 (2007). A role for SUMO proteins in telomerase-mediated telomere elongation is first shown here. · DOI
  83. Kanoh, J. et al. The fission yeast spSet1p is a histone H3-K4 methyltransferase that functions in telomere maintenance and DNA repair in an ATM kinase Rad3-dependent pathway. J. Mol. Biol. 326, 1081–1094 (2003). · DOI
  84. Peters, A. H. et al. Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107, 323–337 (2001). · DOI · Paper page
  85. Schotta, G. et al. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev 18, 1251–1262 (2004). · DOI · Paper page
  86. Kourmouli, N. et al. Heterochromatin and tri-methylated lysine 20 of histone 4 in mammals. J. Cell Sci. 117, 2491–2501 (2004). · DOI
  87. Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116–120 (2001). · DOI · Paper page
  88. Benetti, R., Garcia-Cao, M. & Blasco, M. A. Telomere length regulates the epigenetic status of mammalian telomeres and subtelomeres. Nature Genet. 39, 243–250 (2007). Shows for the first time that telomere shortening to a critical length in mammals results in loss of histone and DNA methylation at mammalian telomeres and subtelomeres, concomitant with increased histone acetylation. · DOI
  89. Netzer, C. et al. SALL1, the gene mutated in Townes–Brocks syndrome, encodes a transcriptional repressor which interacts with TRF1/PIN2 and localizes to pericentromeric heterochromatin. Hum. Mol. Genet. 10, 3017–3024 (2001). · DOI
  90. Kaminker, P. et al. Higher-order nuclear organization in growth arrest of human mammary epithelial cells: a novel role for telomere-associated protein TIN2. J Cell Sci. 118, 1321–1330 (2005). · DOI
  91. Jones, P. A. & Baylin, S. B. The fundamental role of epigenetic events in cancer. Nature Rev. Genet. 3, 415–428 (2002). · DOI · Paper page
  92. Dominguez-Bendala, J. & McWhir, J. Enhanced gene targeting frequency in ES cells with low genomic methylation levels. Transgenic Res. 13, 69–74 (2004). · DOI
  93. Maloisel, L. & Rossignol, J. L. Suppression of crossing-over by DNA methylation in Ascobolus. Genes Dev. 12, 1381–1389 (1998). · DOI
  94. Bender, J. Cytosine methylation of repeated sequences in eukaryotes: the role of DNA pairing. Trends Biochem. Sci. 23, 252–256 (1998). · DOI
  95. Pedram, M. et al. Telomere position effect and silencing of transgenes near telomeres in the mouse. Mol. Cell. Biol. 26, 1865–1878 (2006). · DOI
  96. Steinert, S., Shay, J. W. & Wright, W. E. Modification of subtelomeric DNA. Mol. Cell. Biol. 24, 4571–4580 (2004). · DOI
  97. Okano, M., Bell, D. W., Haber, D. A. & Li, E. DNA methyltransferases DNMT3a and DNMT3b are essential for de novo methylation and mammalian development. Cell 99, 247–257 (1999). · DOI · Paper page
  98. Okano, M., Xie, S. & Li, E. Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases. Nature Genet. 19, 219–220 (1998). · DOI
  99. Chen, T., Tsujimoto, N. & Li, E. The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA methylation to the major satellite repeats at pericentric heterochromatin. Mol. Cell. Biol. 24, 9048–9058 (2004). · DOI
  100. Ofir, R., Wong, A. C., McDermid, H. E., Skorecki, K. L. & Selig, S. Position effect of human telomeric repeats on replication timing. Proc. Natl Acad. Sci. USA 96, 11434–11439 (1999). · DOI
  101. Jiang, G. et al. Testing the position-effect variegation hypothesis for facioscapulohumeral muscular dystrophy by analysis of histone modification and gene expression in subtelomeric 4q. Hum. Mol. Genet. 12, 2909–2921 (2003). · DOI
  102. Bayne, R. A. L. et al. Sandwiching of a gene within 12 kb of a functional telomere and alpha satellite does not result in silencing. Hum Mol Genet. 3, 539–546 (1994). · DOI
  103. Wright, W. E., Tesmer, V. M., Liao, M. L., & Shay, J. W. Normal human telomeres are not late replicating. Exp. Cell Res. 251, 492–499 (1999). · DOI
  104. Ancelin, K. et al. Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2. Mol. Cell. Biol. 22, 3474–3487 (2002). · DOI
  105. Loayza, D. & De Lange, T. POT1 as a terminal transducer of TRF1 telomere length control. Nature 423, 1013–1018 (2003). · DOI
  106. Wang, R. C., Smogorzewska, A. & de Lange, T. Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119, 355–368 (2004). · DOI
  107. Dynek, J. N. & Smith, S. Resolution of sister telomere association is required for progression through mitosis. Science 304, 97–100 (2004). · DOI
  108. Buck, S. W. & Shore, D. Action of a RAP1 carboxy-terminal silencing domain reveals an underlying competition between HMR and telomeres in yeast. Genes Dev. 9, 370–384 (1995). · DOI
  109. Wiley, E. A. & Zakian, V. A. Extra telomeres, but not internal tracts of telomeric DNA, reduce transcriptional repression at Saccharomyces telomeres. Genetics 139, 67–79 (1995). · DOI
  110. Marcand, S., Brevet, V. & Gilson, E. Progressive cis-inhibition of telomerase upon telomere elongation. EMBO J. 18, 3509–3519 (1999). · DOI
  111. Teixeira, M. T., Arneric, M., Sperisen, P. & Lingner, J. Telomere length homeostasis is achieved via a switch between telomerase-extendible and -nonextendible states. Cell 117, 323–335 (2004). This work shows that budding yeast telomerase activity preferentially acts on the shortest telomeres. · DOI · Paper page
  112. Xu, G. L. et al. Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene. Nature 402, 187–191 (1999). · DOI
  113. Amir, R. E. et al. Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2. Nature Genet. 23, 185–188 (1999). · DOI · Paper page
  114. Haigis, M. C. et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β-cells. Cell 126, 941–954 (2006). · DOI · Paper page
  115. Mostoslavsky, R. et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124, 315–329 (2006). · DOI · Paper page
  116. Chua, K. F. et al. Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress. Cell Metab. 2, 67–76 (2005). · DOI
  117. Roth, W. et al. PIASy-deficient mice display modest defects in IFN and Wnt signaling. J. Immunol. 173, 6189–6199 (2004). · DOI
  118. Nacerddine, K. et al. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev. Cell. 9, 769–779 (2005). · DOI
  119. Marciniak, R. A. et al. A novel telomere structure in a human alternative lengthening of telomeres cell line. Cancer Res. 65, 2730–2737 (2005). · DOI

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Metadata

Authors
Blasco, M. A.
Venue
Nature Reviews Genetics
Published
2007-04
Volume
8
Issue
4
Pages
299-309
ISSN
  • 1471-0056
  • 1471-0064
Cited by
600
References
24
Language
en

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