Involvement of the Silencer and UAS Binding Protein RAP1 in Regulation of Telomere Length

Lustig, Arthur J.; Kurtz, Stephen E.; Shore, David

doi:10.1126/science.2237406

Cited by 314 publications

(271 citation statements)

References 36 publications

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“…Direct evidence that telomeric DNA protects free DNA ends from such degradation came from experiments placing a short stretch of telomeric DNA next to the break site, which limited this rapid degradation, even in the absence of telomerase (Diede and Gottschling, 1999). De novo telomere formation on linear plasmids transformed into S. cerevisiae is enhanced by even short terminal sequences of telomeric DNA (Lustig et al, 1990). This provides further molecular evidence supporting the notion that the action of DNA damage proteins is limited by telomeric sequences.…”

Section: Dna Damage Response Proteins and Telomere Maintenancesupporting

confidence: 63%

New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin

2002

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Telomeres are stabilized, and telomeric DNA is replenished, by the action of the ribonucleoprotein reverse transcriptase telomerase. Telomere capping functions include the ability of telomeres to protect chromosome ends from cellular DNA-damage responses such as cell cycle arrest or apoptosis. This property of telomeres is especially important for cancer cells, which continue proliferating despite chromosome aberrations. Telomere capping is in¯uenced by multiple, mutually reinforcing factors including telomere length, although telomere length is only one of several determinants of telomere functionality. For example, many cancer cells express high levels of telomerase yet maintain relatively short telomeres. We consider three aspects of telomere capping that have emerged relatively recently: (1) a new role for telomerase in telomere capping independent of its function in telomere elongation. Support for this novel function comes from experiments showing an increase in replicative potential with the reactivation of telomerase, without net telomere lengthening; (2) the role at telomeres of DNA damage proteins. We propose a model in which two factors speci®cally target telomeres for the action of telomerase, as opposed to recombination or non-homologous end-joining: binding by telomeric proteins that limits DNA damage responses at telomeres, and the a nity of the telomerase RNP for telomeric proteins and DNA; and (3) we discuss a potential protective role of ampli®ed subtelomeric DNAs, which may aid capping of telomeres maintained by nontelomerase based mechanisms through the formation of heterochromatin.

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Section: Dna Damage Response Proteins and Telomere Maintenancesupporting

confidence: 63%

New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin

2002

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“…In Oxytricha and Euplotes, the protruding G-rich repeats are bound by a telomere capping complex which protects telomeres from ligation and exonucleolytic attack in vitro (Lipps et al, 1982;Gottschling and Cech, 1984;Gottsc.hling and Zakian, 1986;Price andCech, 1987, 1989;Raghuraman et al, 1989;Price, 1990). Telomere capping complexes have not been identified in other organisms, but genetic and biochemical experiments suggest that the telomeres of Saccharomyces cerevisiae interact with the repressor/activator protein RAPI (Berman et al, 1986;Buchman et al, 1988;Longtine et al, 1989;Conrad et al, 1990;Lustig et al, 1990). The function of the RAPI -telomere association is not known.…”

Section: Introductionmentioning

confidence: 99%

Human telomeres are attached to the nuclear matrix.

1992

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This report shows that human telomeres are tightly associated with the nuclear matrix. Telomere attachment is observed in several cell types and in all stages of interphase. Mapping experiments show that telomeres are anchored via their TTAGGG repeats; a subtelomeric repeat located immediately proximal to the telomeric TTAGGG repeats is quantitatively released from the nuclear matrix by restriction endonuclease cleavage. TTAGGG repeats introduced at chromosome-internal sites by DNA transfection do not behave as matrix attached loci, suggesting that the telomeric position of the repeats is required for their interaction with the nuclear matrix. These findings are consistent with the idea that telomeres function as a nucleoprotein complex.

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“…The telomere length is around 300 bp. Native chromosome ends in S. cerevisiae have a number of subtelomeric (Lustig et al 1990). Rap1 also binds chromosome internal sites acting as positive transcriptional regulator of genes involved in growth control.…”

Section: S Cerevisiaementioning

confidence: 99%

Replication of Telomeres and the Regulation of Telomerase

Pfeiffer

Lingner

2013

Cold Spring Harbor Perspectives in Biology

109

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Telomeres are the physical ends of eukaryotic chromosomes. They protect chromosome ends from DNA degradation, recombination, and DNA end fusions, and they are important for nuclear architecture. Telomeres provide a mechanism for their replication by semiconservative DNA replication and length maintenance by telomerase. Through telomerase repression and induced telomere shortening, telomeres provide the means to regulate cellular life span. In this review, we introduce the current knowledge on telomere composition and structure. We then discuss in depth the current understanding of how telomere components mediate their function during semiconservative DNA replication and how telomerase is regulated at the end of the chromosome. We focus our discussion on the telomeres from mammals and the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.

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Involvement of the Silencer and UAS Binding Protein RAP1 in Regulation of Telomere Length

Cited by 314 publications

References 36 publications

New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin

New ways not to make ends meet: telomerase, DNA damage proteins and heterochromatin

Human telomeres are attached to the nuclear matrix.

Replication of Telomeres and the Regulation of Telomerase

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