Nucleic Acids Research, 1993, Vol. 21, No. 4 999-1006
© 1993
MOLECULAR BIOLOGY |
Three new members of the RNP protein family in Xenopus
Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health Bethesda, MD 20892, USA
Received September 28, 1992. Revised January 7, 1993. Accepted January 7, 1993.
Many RNP proteins contain one or more copies of the RNA recognition motif (RRM) and are thought to be involved in cellular RNA metabolism. We have previously characterized in Xenopus a nervous system specific gene, nrp1, that is more simliar to the hnRNP A/B proteins than to other known proteins (K.Richter, P.J.Good, and I.B.Dawid (1990), New Blol. 2,556-565). PCR amplification with degenerate primers was used to identify additional cDNAs encoding two RRMs in Xenopus. Three previously uncharacterlzed genes were identified. Two genes encode hnRNP A/B proteins with two RRMs and a glycine-rich domain. One of these is the Xenopus homoiog of the human A2/B1 gene; the other, named hnRNP A3, is similar to both the A1 and A2 hnRNP genes. The Xenopus hnRNP A1, A2 and A3 genes are expressed throughout development and in all adult tissues. Multiple protein isoforms for the hnRNP A2 gene are predicted that differ by the insertion of short peptide sequences in the glycine-rich domain. The third newly isolated gene, named xrp1, encodes a protein that is related by sequence to the nrpl protein but is expressed ubiquitously. Despite the similarity to nuclear RNP proteins, both the nrp1 and xrp1 proteins are localized to the cytoplasm in the Xenopus oocyte. The xrp1 gene may have a function in all cells that is similar to that executed by nrp1 specifically within the nervous system.
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