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Nucleic Acids Research, 2001, Vol. 29, No. 5 1200-1207
© 2001 Oxford University Press

Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3'->5' exonuclease activity

Hiroto Izumi, Toshihiro Imamura, Gunji Nagatani, Tomoko Ise, Tadashi Murakami, Hidetaka Uramoto, Takayuki Torigoe, Hiroshi Ishiguchi, Yoichiro Yoshida, Minoru Nomoto, Tatsuro Okamoto1, Takeshi Uchiumi1, Michihiko Kuwano1, Keiko Funa2 and Kimitoshi Kohno*

Department of Molecular Biology, University of Occupational and Environmental Health, 1-1 Iseigaoka Yahatanisi-ku, Kitakyushu 807-8555, Japan, 1Department of Medical Biochemistry, Graduate School of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan and 2Department of Medical Cell Biology, Institute of Anatomy and Cell Biology, Göteborg University, Box 420, SE-405 30 Göteborg, Sweden

We have previously shown that Y box-binding protein-1 (YB-1) binds preferentially to cisplatin-modified Y box sequences. Based on structural and biochemical data, we predicted that this protein binds single-stranded nucleic acids. In the present study we confirmed the prediction and also discovered some unexpected functional features of YB-1. We found that the cold shock domain of the protein is necessary but not sufficient for double-stranded DNA binding while the C-tail domain interacts with both single-stranded DNA and RNA independently of the cold shock domain. In an in vitro translation system the C-tail domain of the protein inhibited translation but the cold shock domain did not. Both in vitro pull-down and in vivo co-immunoprecipitation assays revealed that YB-1 can form a homodimer. Deletion analysis mapped the C-tail domain of the protein as the region of homodimerization. We also characterized an intrinsic 3'->5' DNA exonuclease activity of the protein. The region between residues 51 and 205 of its 324-amino acid extent is required for full exonuclease activity. Our findings suggest that YB-1 functions in regulating DNA/RNA transactions and that these actions involve different domains.

* To whom correspondence should be addressed. Tel: +81 93 691 7423; Fax: +81 93 692 2766; Email: k-kohno{at}med.uoeh-u.ac.jp


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