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Papers In Press, published online ahead of print February 21, 2002
J. Biol. Chem, 10.1074/jbc.C100764200
Submitted on December 27, 2001
Revised on February 15, 2002
Accepted on February 20, 2002
University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
Corresponding Author: rstansel{at}nc.rr.com
The interaction of p53 with a human model telomere in vitro was examined by electron microscopy. p53 demonstrated a sequence-independent affinity for telomeric DNA in vitro, localizing to the 3’ single strand overhang and the t-loop junction both in the presence and absence of associated TRF2. Binding was not observed above background along the duplex telomeric repeats. The efficiency of TRF2 catalyzed t-loop formation on the model DNA however was increased two-fold in the presence of p53 while a variety of single strand or Holliday junction-binding proteins did not facilitate t-loop formation. These results suggest that p53 has an active role in telomere maintenance and structure through association with the t-loop junction.
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