Nucleic Acids Research, 1994, Vol. 22, No. 25 5582-5589
© 1994
Articles |
Binding of Y-box proteins to RNA: involvement of different protein domains
School of Biological and Medical Sciences, University of St Andrews St Andrews, Fife KY16 9TS, UK
*To whom correspondence should be addressed
Received September 27, 1994. Revised November 18, 1994. Accepted November 18, 1994.
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 phosphoryl-atlon. 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 MgCl² 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.
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