Role of the telomeric DNA‐binding protein TRF2 in the stability of human chromosome ends
A major issue in telomere research is to understand how the integrity of chromosome ends is
preserved. A recent study shows that expression of a dominant‐negative form of the human
telomeric protein TRF2 increases the number of chromosome fusions in immortalized cells
and decreases the quantity of G‐rich telomeric DNA 3'overhang, the G tail.(1) Consequently,
TRF2 appears to control the structure of the very end of the chromosomal DNA molecule and
to prevent recombination between two telomeres. Remarkably, the same study reveals a …
preserved. A recent study shows that expression of a dominant‐negative form of the human
telomeric protein TRF2 increases the number of chromosome fusions in immortalized cells
and decreases the quantity of G‐rich telomeric DNA 3'overhang, the G tail.(1) Consequently,
TRF2 appears to control the structure of the very end of the chromosomal DNA molecule and
to prevent recombination between two telomeres. Remarkably, the same study reveals a …
Abstract
A major issue in telomere research is to understand how the integrity of chromosome ends is preserved. A recent study shows that expression of a dominant‐negative form of the human telomeric protein TRF2 increases the number of chromosome fusions in immortalized cells and decreases the quantity of G‐rich telomeric DNA 3' overhang, the G tail.(1) Consequently, TRF2 appears to control the structure of the very end of the chromosomal DNA molecule and to prevent recombination between two telomeres. Remarkably, the same study reveals a potential role of TRF2 in cell division control. BioEssays 20:879–883, 1998. © 1998 John Wiley & Sons, Inc.
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