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Vol. 14, Issue 2, 556-570, February 2003
Department of Biochemistry and Biophysics, University of
California, San Francisco, San Francisco, California 94143-0448
In Saccharomyces cerevisiae, telomeric DNA is
protected by a nonnucleosomal protein complex, tethered by the protein
Rap1. Rif and Sir proteins, which interact with Rap1p, are thought to have further interactions with conventional nucleosomic chromatin to
create a repressive structure that protects the chromosome end. We
showed by microarray analysis that Rif1p association with the
chromosome ends extends to subtelomeric regions many kilobases internal
to the terminal telomeric repeats and correlates strongly with the
previously determined genomic footprints of Rap1p and the Sir2-4
proteins in these regions. Although the end-protection function of
telomeres is essential for genomic stability, telomeric DNA must also
be copied by the conventional DNA replication machinery and replenished
by telomerase, suggesting that transient remodeling of the telomeric
chromatin might result in distinct protein complexes at different
stages of the cell cycle. Using chromatin immunoprecipitation, we
monitored the association of Rap1p, Rif1p, Rif2p, and the protein component of telomerase, Est2p, with telomeric DNA through the cell
cycle. We provide evidence for dynamic remodeling of these components
at telomeres.
This article contains supplementary data. The supplementary data is
available at www.molbiolcell.org.
*
Corresponding author. E-mail address: telomer{at}itsa.ucsf.edu.
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