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Human Molecular Genetics Advance Access published online on June 30, 2004
Human Molecular Genetics, doi:10.1093/hmg/ddh193
© 2004 by Oxford University Press
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Article

Association and regulation of the BLM helicase by the telomere proteins TRF1 and TRF2

Kate Lillard-Wetherell 1, Amrita Machwe 2, Gregory T. Langland 1, Kelly A. Combs 1, Gregory K. Behbehani 1, Steven A. Schonberg 3, James German 4, John J. Turchi 5, David K. Orren 2, Joanna Groden 6*

1 Department of Molecular Genetics, Biochemistry and Microbiology, and Howard Hughes Medical Institute, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267
2 Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40536
3 Department of Pediatrics, George Washington University School of Medicine, Washington D.C. 20052 and American Quest Laboratories, Inc., Chantilly, Virginia 20153
4 Department of Pediatrics, Weill Medical College of Cornell University, New York, New York 10021
5 Department of Biochemistry and Molecular Biology, Wright State University School of Medicine, Dayton, Ohio 45435
6 Howard Hughes Medical Institute and Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, Ohio 45267-0524

* To whom correspondence should be addressed. E-mail: joanna.groden{at}uc.edu.


  Abstract

In addition to increased DNA-strand exchange, a cytogenetic feature of cells lacking the RecQ-like BLM helicase is a tendency for telomeres to associate. We also report additional cellular and biochemical evidence for the role of BLM in telomere maintenance. BLM co-localizes and complexes with the telomere repeat protein TRF2 in cells that employ the recombination-mediated mechanism of telomere lengthening known as ALT. BLM co-localizes with TRF2 in foci actively synthesizing DNA during late S and G2/M; co-localization increases in late S and G2/M when ALT is thought to occur. Additionally, TRF1 and TRF2 interact directly with BLM and regulate BLM unwinding activity in vitro. While TRF2 stimulates BLM unwinding of telomeric and non-telomeric substrates, TRF1 inhibits BLM unwinding of telomeric substrates only. Finally, TRF2 stimulates BLM unwinding with equimolar concentrations of TRF1, but not when TRF1 is added in molar excess. These data suggest a function for BLM in recombination-mediated telomere lengthening and support a model for the coordinated regulation of BLM activity at telomeres by TRF1 and TRF2.


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