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Originally published In Press as doi:10.1074/jbc.C000390200 on July 25, 2000

J. Biol. Chem., Vol. 275, Issue 39, 30618-30622, September 29, 2000
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NBS1 and TRF1 Colocalize at Promyelocytic Leukemia Bodies during Late S/G2 Phases in Immortalized Telomerase-negative Cells
IMPLICATION OF NBS1 IN ALTERNATIVE LENGTHENING OF TELOMERES*

Guikai WuDagger , Wen-Hwa Lee, and Phang-Lang Chen§

From the Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245

Nijmegen breakage syndrome, a chromosomal instability disorder, is characterized in part by cellular hypersensitivity to ionizing radiation. The NBS1 gene product, p95 (NBS1 or nibrin) forms a complex with Rad50 and Mre11. Cells deficient in the formation of this complex are defective in DNA double-strand break repair, cell cycle checkpoint control, and telomere length maintenance. How the NBS1 complex is involved in telomere length maintenance remains unclear. Here we show that the C-terminal region of NBS1 interacts directly with a telomere repeat binding factor, TRF1, by both yeast two-hybrid and in vivo DNA-coimmunoprecipitation assays. NBS1 and Mre11 colocalize with TRF1 at promyelocytic leukemia (PML) nuclear bodies in immortalized telomerase-negative cell lines, but rarely in telomerase-positive cell lines. The translocation of NBS1 to PML bodies occurs specifically during late S to G2 phases of the cell cycle and coincides with active DNA synthesis in these NBS1-containing PML bodies. These results suggest that NBS1 may be involved in alternative lengthening of telomeres in telomerase-negative immortalized cells.

* This work was supported in part by National Institutes of Health Grants CA85605 (to P. L. C.) and CA81020 (to W. H. L.), and a grant from the V Foundation for Cancer Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by Predoctoral Training Grant DAMD17-99-1-9402 from the Department of Defense.

§ To whom correspondence should be addressed: Dept. of Molecular Medicine and Inst. Of Biotechnology, University of Texas Health Science Center at San Antonio, 15355 Lambda Dr., San Antonio, TX 78245. Tel.: 210-567-7353; Fax: 210-567-7377; E-mail: chenp0@uthscsa.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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