Binding of Y-box proteins to RNA: Involvement of different protein domains
Ladomery, M. and Sommerville, J. (1994) Binding of Y-box proteins to RNA: Involvement of different protein domains. Nucleic Acids Research, 22 (25). pp. 5582-5589. ISSN 0305-1048
Full text not available from this repository
Publisher's URL: http://nar.oxfordjournals.org/
Eukaryotlc Y-box proteins are reported to interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins. The modular structure of Y-box proteins Includes a highly conserved N-termlnal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) plus four basic C-termlnal domains containing arginine clusters and aromatic residues. In addition, the basic domains are separated by acidic regions which contain several potential sites for serine/threonlne phosphorylatlon. The Interaction of Y-box proteins, isolated from Xenopus oocytes (FRGY2 type), with RNA molecules has been studied by UV crossllnklng and protein fragmentation. We have identified two distinct binding activities. The CSD interacts preferentially with the polypurlnes poly(A.G) and poly(G) but not poly (A), this activity being sensitive to 5 mM MgClj but not to 5 mM spermldlne. In the presence of 1 mM MgCI2 or 1 mM spermldlne, the basic domains interact preferentially with poly(C,U), this activity being sensitive to 0.5 M NaCI. Binding of the basic domains is also sensitive to low concentrations of heparln. The basic domains can be crossllnked individually to labelled RNA. These results are discussed with reference to the various specificities noted In the binding of Y-box proteins to RNA and DNA.