Mammalian Telomeres End in a Large Duplex Loop
@article{Griffith1999MammalianTE, title={Mammalian Telomeres End in a Large Duplex Loop}, author={Jack D. Griffith and Laurey D. Comeau and S I Rosenfield and Rachel M. Stansel and Alessandro Bianchi and Heidi Moss and Titia de Lange}, journal={Cell}, year={1999}, volume={97}, pages={503-514} }
2,381 Citations
Telomere Organization and Nuclear Movements
- Biology
- 2004
The telomeric cap structure prevents DNA damage checkpoint and repair mechanisms from treating telomeres as breaks, and their length is controlled by positive and negative regulators for the telomerase.
Telomeric 3′-overhang length is associated with the size of telomeres
- BiologyExperimental Gerontology
- 2008
Strand-Specific Postreplicative Processing of Mammalian Telomeres
- Biology, ChemistryScience
- 2001
It is shown that TRF2-mediated end-capping occurs after telomere replication, a crucial difference in postreplicative processing of telomeres that is linked to their mode of replication.
Interactions of TRF2 with model telomeric ends.
- Biology, ChemistryBiochemical and biophysical research communications
- 2007
Interstitial telomeric loops and implications of the interaction between TRF2 and lamin A/C.
- BiologyDifferentiation; research in biological diversity
- 2018
Taz1 Binding to a Fission Yeast Model Telomere
- BiologyJournal of Biological Chemistry
- 2004
In vitro results suggest that Taz1p binds the 3′ overhang then extrudes a loop that grows in size as the donut slides along the duplex DNA, resembling the pattern of TRF1 binding.
A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends.
- Biology, ChemistryMolecular cell
- 2007
Importance of TRF1 for Functional Telomere Structure*
- Biology, ChemistryJournal of Biological Chemistry
- 2004
End-to-end fusions with detectable telomere signals at fusion points accumulated in TRF1-deficient cells strongly suggest that TRF 1 interacts with other telomer-binding molecules and integrates into the functional telomeres structure.
Telomere-dependent chromosomal instability.
- BiologyThe journal of investigative dermatology. Symposium proceedings
- 2005
Evidence is provided that in a length-independent manner telomeres can confer to genomic instability by forming telomericaggregates which through chromosomal dys-locations contribute to chromosomal aberrations.
References
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Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase, demonstrating that human telomeres form a specialized nucleoprotein complex.
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Affinity-purified antibodies specific for anti-TRF2 label the telomeres of intact human chromosomes, strengthening the correlation between occurrence of telobox and telomere-repeat recognition in vivo.
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It is proposed that the binding of TRF1 controls telomere length in cis by inhibiting the action of telomerase at the ends of individual telomeres, and shown that the human telomeric-repeat binding factor TRF 1 is involved in this regulation.
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It is suggested that TRF binds along the length of mammalian telomeres, indicating thatTRF preferentially recognizes the telomeric repeat sequence present at mammalian chromosome ends.
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The structure of in vitro complexes formed between telomeric DNA and TRF1 as deduced by electron microscopy suggests that this protein may have an architectural role at telomeres and the possibility that TRf1-dependent changes in the conformation oftelomeres are involved in the regulation of telomere length.
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Human telomeres contain two distinct Myb–related proteins, TRF1 and TRF2
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The cloning of TRF2 is reported, a distant homologue of TRf1 that carries a very similar Myb-related DNA-binding motif and a large TRF1-related dimerization domain near its N terminus that suggests these factors have distinct functions at telomeres.
Structure, subnuclear distribution, and nuclear matrix association of the mammalian telomeric complex
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Biochemical and ultrastructural data presented here show that the telomeric DNA and TRF colocalize in individual, condensed structures in the nuclear matrix, consistent with the view that mammalian telomeres form nuclear matrix- associated, TRF-containing higher order complexes at dispersed sites throughout the nuclear volume.
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The amount and length of telomeric DNA in human fibroblasts does in fact decrease as a function of serial passage during ageing in vitro and possibly in vivo.