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Nuclear poly(A) polymerase (PAP) polyadenylates nascent mRNAs, promoting their nuclear export, stability, and translation, while the related cytoplasmic polymerase GLD-2 activates translation of deadenylated mRNAs. Here we characterize the biochemical activity of fission yeast Schizosaccharomyces pombe Cid1, a putative cytoplasmic PAP implicated in cell cycle checkpoint controls. Surprisingly, Cid1 has robust poly(U) polymerase activity in vitro, especially when isolated in native multiprotein complexes. Furthermore, we found that upon S-phase arrest, the 3' ends of actin mRNAs were posttranscriptionally uridylated in a Cid1-dependent manner. Finally, Hs2 (ZCCHC6), a human ortholog of Cid1, shows similar activity. These data suggest that uridylation of mRNA forms the basis of an evolutionarily conserved mechanism of gene regulation.

Original publication




Journal article


Mol Cell Biol

Publication Date





3612 - 3624


Actins, Adenosine Triphosphate, Base Sequence, Cell Cycle, Humans, Molecular Sequence Data, Multienzyme Complexes, Nucleotidyltransferases, Poly A, Polynucleotide Adenylyltransferase, RNA, Messenger, Recombinant Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Uridine Monophosphate