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[Cancer Research 60, 1162-1167, March 1, 2000]
© 2000 American Association for Cancer Research

Advances in Brief

Association of the Bloom Syndrome Protein with Topoisomerase III{alpha} in Somatic and Meiotic Cells1

F. Brad Johnson2, David B. Lombard2, Norma F. Neff, Mary-Ann Mastrangelo, William Dewolf, Nathan A. Ellis, Robert A. Marciniak, Yizhong Yin, Rudolf Jaenisch and Leonard Guarente3

Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 [F. B. J., D. B. L., R. A. M., L. G.]; Department of Pathology, Brigham and Women’s Hospital, Boston, Massachusetts 02115 [F. B. J.]; Division of Hematology-Oncology, Massachusetts General Hospital, Boston, Massachusetts 02114 [R. A. M.]; Laboratory of Molecular Genetics, New York Blood Center, New York, New York 10021 [N. F. N.]; Whitehead Institute, Cambridge, Massachusetts 02142 [M-A. M., R. J.]; Beth Israel/Deaconess Medical Center, Boston, Massachusetts 02215 [W. D., Y. Y.]; and Laboratory of Cancer Susceptibility, Memorial Sloan-Kettering Cancer Research Center, New York, New York 10021 [N. A. E.]

Bloom syndrome (BS) is characterized by genomic instability and cancer susceptibility caused by defects in BLM, a DNA helicase of the RecQ-family (J. German and N. A. Ellis, The Genetic Basis of Human Cancer, pp. 301–316, 1998). RecQ helicases and topoisomerase III proteins interact physically and functionally in yeast (S. Gangloff et al., Mol. Cell. Biol., 14: 8391–8398, 1994) and in Escherichia coli can function together to enable passage of double-stranded DNA (F. G. Harmon et al., Mol. Cell, 3: 611–620, 1999). We demonstrate in somatic and meiotic human cells an association between BLM and topoisomerase III{alpha}. These proteins colocalize in promyelocytic leukemia protein nuclear bodies, and this localization is disrupted in BS cells. Thus, mechanisms by which RecQ helicases and topoisomerase III proteins cooperate to maintain genomic stability in model organisms likely apply to humans.




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