Efficient RNA Polyuridylation by Noncanonical Poly(A) Polymerases

Author:

Rissland Olivia S.1,Mikulasova Andrea1,Norbury Chris J.1

Affiliation:

1. Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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