Abstract
The Xenopus Y-box protein FRGY2 has a role in the translational silencing of masked maternal mRNA. Here, we determine that FRGY2 will recognize specific RNA sequences. The evolutionarily conserved nucleic acid-binding cold shock domain is required for sequence-specific interactions with RNA. However, RNA binding by FRGY2 is facilitated by N- and C-terminal regions flanking the cold shock domain. The hydrophilic C-terminal tail domain of FRGY2 interacts with RNA independent of the cold shock domain but does not determine sequence specificity. Thus, both sequence-specific and nonspecific RNA recognition domains are contained within the FRGY2 protein.
Highlights
The Xenopus Y-box protein FRGY2 has a role in the translational silencing of masked maternal mRNA
The evolutionarily conserved nucleic acid-binding cold shock domain is required for sequence-specific interactions with RNA
FRGY2 has an active role in facilitating the translational silencing or masking of maternal mRNA (Richter and Smith, 1984; Ranjan et al, 1993; Bouvet and Wolffe, 1994)
Summary
(Received for publication, July 7, 1995, and in revised form, September 5, 1995). Philippe Bouvet‡§, Ken Matsumoto‡, and Alan P. The evolutionarily conserved nucleic acid-binding cold shock domain is required for sequence-specific interactions with RNA. The hydrophilic C-terminal tail domain of FRGY2 interacts with RNA independent of the cold shock domain but does not determine sequence specificity. Both sequence-specific and nonspecific RNA recognition domains are contained within the FRGY2 protein. The Y-box proteins contain a nucleic acid-binding domain conserved between prokaryotic and eukaryotic organisms (reviewed by Wolffe (1994a, 1994b)). The prokaryotic Y-box proteins regulate the cold shock response (Goldstein et al, 1990; La Teana et al, 1991; Jones et al, 1992) These proteins contain a single nucleic acid-binding structure known as the cold shock domain (CSD) (Wistow, 1990). We discuss the significance of these observations for the potential roles of FRGY2 in transcriptional and translational control
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