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MBC in Press, published online ahead of print May 14, 2004
Mol. Biol. Cell 10.1091/mbc.E04-03-0227

A more recent version of this article appeared on July 1, 2004
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Submitted on March 17, 2004
Revised on April 27, 2004
Accepted on April 29, 2004

Cell cycle-dependent regulation of a human DNA helicase that localizes in DNA damage foci

Jinming Gu{dagger}{sect}, Xiaobo Xia{ddagger}{sect}, Peijun Yan{dagger}{sect}, Hanjian Liu{dagger}{sect}, Vladimir N. Podust{dagger}{sect}, Albert B. Reynolds{ddagger}{sect}, and Ellen Fanning{dagger}{sect}*

{dagger}Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235 USA, {ddagger}Department of Cancer Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 USA, and {sect}Vanderbilt-Ingram Cancer Center, Nashville, TN 37232 USA

Monitoring Editor: Keith Yamamoto

Mutational studies of human DNA helicase B (HDHB) have suggested that its activity is critical for the G1/S transition of the cell cycle, but the nature of its role remains unknown. In this study, we show that during G1, ectopically expressed HDHB localizes in nuclear foci induced by DNA damaging agents and that this focal pattern requires active HDHB. During S and G2/M, HDHB localizes primarily in the cytoplasm. A carboxy-terminal domain from HDHB confers cell cycle-dependent localization, but not the focal pattern, to a reporter protein. A cluster of potential cyclin-dependent kinase phosphorylation sites in this domain was modified at the G1/S transition and maintained through G2/M of the cell cycle in vivo, coincident with nuclear export of HDHB. Serine 967 of HDHB was the major site phosphorylated in vivo and in vitro by cyclin-dependent kinases. Mutational analysis demonstrated that phosphorylation of serine 967 is crucial in regulating the subcellular localization of ectopically expressed HDHB. We propose that the helicase of HDHB operates primarily during G1 to process endogenous DNA damage before the G1/S transition, and is largely sequestered in the cytoplasm during S/G2.

*Corresponding author. E-mail address: Ellen.Fanning{at}VANDERBILT.EDU




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