Nucleic Acids Research, Vol 26, Issue 7 1597-1604, Copyright © 1998 by Oxford University Press
C Bai and PP Tolias
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.
ARTICLES
Drosophila clipper/CPSF 30K is a post-transcriptionally regulated nuclear protein that binds RNA containing GC clusters
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