Drosophila clipper/CPSF 30K is a post-transcriptionally regulated nuclear protein that binds RNA containing GC clusters

An essential component of the mammalian pre-mRNA 3′-end processing machinery is a multimeric protein complex known as cleavage and polyadenylation specificity factor (CPSF). The Drosophila melanogaster gene, clipper (clp), encodes a homolog of the CPSF 30K subunit. We have shown previously that CLP...

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Bibliographic Details
Published inNucleic acids research Vol. 26; no. 7; pp. 1597 - 1604
Main Authors Bai, C, Tolias, P.P
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.04.1998
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Summary:An essential component of the mammalian pre-mRNA 3′-end processing machinery is a multimeric protein complex known as cleavage and polyadenylation specificity factor (CPSF). The Drosophila melanogaster gene, clipper (clp), encodes a homolog of the CPSF 30K subunit. We have shown previously that CLP possesses N-terminal endoribonucleolytic activity and that the relative expression of its mRNA fluctuates during fly development. In the present study, we report that CLP's C-terminus, containing two CCHC zinc knuckles, confers a binding preference for RNAs that contain G- and/or C-rich clusters. We also show, for the first time, that a member of the highly conserved CPSF 30K family is a nuclear and developmentally regulated protein. Though clp transcripts are detectable throughout embryogenesis, CLP protein is not present. We demonstrate that post-transcriptional regulation of clp mRNA in the embryo occurs by a process that does not involve poly(A) tail length shortening. Thus, a key component of the pre-mRNA 3′-end processing machinery is subject to post-transcriptional regulation during development. These results support the existence of a distinct mechanism controlling eukaryotic gene expression through the regulated processing of pre-mRNAs in the nucleus.
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ISSN:0305-1048
1362-4962
DOI:10.1093/nar/26.7.1597