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Human Molecular Genetics Advance Access originally published online on June 30, 2004
Human Molecular Genetics 2004 13(17):1919-1932; doi:10.1093/hmg/ddh193
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Human Molecular Genetics, Vol. 13, No. 17 © Oxford University Press 2004; all rights reserved

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

Kate Lillard-Wetherell1, Amrita Machwe2, Gregory T. Langland1, Kelly A. Combs1, Gregory K. Behbehani1, Steven A. Schonberg3,4, James German5, John J. Turchi6, David K. Orren2 and Joanna Groden1,*

1Department of Molecular Genetics, Biochemistry and Microbiology, Howard Hughes Medical Institute, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA, 2Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40536, USA, 3Department of Pediatrics, George Washington University School of Medicine, Washington DC 20052, USA, 4American Quest Laboratories, Inc., Chantilly, VA 20153, USA, 5Department of Pediatrics, Weill Medical College of Cornell University, New York, NY 10021, USA and 6Department of Biochemistry and Molecular Biology, Wright State University School of Medicine, Dayton, OH 45435, USA

Received April 28, 2004; Revised June 3, 2004; Accepted June 15, 2004

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 (alternative lengthening of telomeres). 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. Whereas 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.

* To whom correspondence should be addressed at: Department of Molecular Genetics, Biochemistry and Microbiology, Howard Hughes Medical Institute, University of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, OH 45267-0524, USA. Tel: +1 5135580088; Email: joanna.groden{at}uc.edu


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