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Science 8 December 1995:
Vol. 270. no. 5242, pp. 1663 - 1667
DOI: 10.1126/science.270.5242.1663

Reports

A Human Telomeric Protein

Laura Chong,  Bas van Steensel,  Dominique Broccoli,  Hediye Erdjument-Bromage,  John Hanish (1),  Paul Tempst,  Titia de Lange (2)

Telomeres are multifunctional elements that shield chromosome ends from degradation and end-to-end fusions, prevent activation of DNA damage checkpoints, and modulate the maintenance of telomeric DNA by telomerase. A major protein component of human telomeres has been identified and cloned. This factor, TRF, contains one Myb-type DNA-binding repeat and an amino-terminal acidic domain. Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase. The presence of TRF along the telomeric TTAGGG repeat array demonstrates that human telomeres form a specialized nucleoprotein complex.


L. Chong, B. van Steensel, D. Broccoli, J. Hanish, T. de Lange, Laboratory for Cell Biology and Genetics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
H. Erdjument-Bromage and P. Tempst, Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.
(1) Present address: Laboratory of Chromosome Structure, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.
(2) To whom correspondence should be addressed. E-mail: delange{at}rockvax.rockefeller.edu


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