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Essential yeast protein with unexpected similarity to subunits of mammalian cleavage and polyadenylation specificity
G Chanfreau1, S M Noble, C Guthrie
1Department of Biochemistry and Biophysics, UCSF School of Medicine, San Francisco, CA 94143-0448. guthrie@cgl.ucsf.edu.
Abstract:
The 3' ends of most eukaryotic messenger RNAs are generated by internal cleavage and polyadenylation. In mammals, there is a strict dependence of both reactions on the sequence AAUAAA, which occurs upstream of polyadenylation [poly(A)] sites and which is recognized by CPSF. In contrast, cis-acting signals for yeast 3'-end generation are highly divergent from those of mammals, suggesting that trans-acting factors other than poly(A) polymerase would not be conserved. The essential yeast protein Brr5/Ysh1 shows sequence similarity to subunits of mammalian CPSF and is required for 3'-end processing in vivo and in vitro. These results demonstrate a structural and functional conservation of the yeast and mammalian 3'-end processing machineries despite a lack of conservation of the cis sequences.