Abstract:
: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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Izumi H,Imamura T,Nagatani G,Ise T,Murakami T,Uramoto H,Torigoe T,Ishiguchi H,Yoshida Y,Nomoto M,Okamoto T,Uchiumi T,Kuwano M,Funa K,Kohno Kdoi
10.1093/nar/29.5.1200keywords:
subject
Has Abstractpub_date
2001-03-01 00:00:00pages
1200-7issue
5eissn
0305-1048issn
1362-4962journal_volume
29pub_type
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