Binding of Y-box proteins to RNA: Involvement of different protein domains

Ladomery, Michael; Sommerville, John

Abstract

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.

• Journal Article Type: Article
• Publication Date: Dec 1, 1994
• Journal: Nucleic Acids Research
• Print ISSN: 0305-1048
• Publisher: Oxford University Press (OUP)
• Peer Reviewed: Peer Reviewed
• Volume: 22
• Issue: 25
• Pages: 5582-5589
• Public URL: https://uwe-repository.worktribe.com/output/1107971
• Publisher URL: http://nar.oxfordjournals.org/