Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The Schizosaccharomyces pombe cytoplasmic protein Cid1 acts as a poly(U) polymerase (PUP). Polyadenylated actin mRNA, a target of this activity, is uridylated upon arrest in S phase and is likely to be one of many such Cid1 targets. This RNA uridylation pathway appears to be conserved, as Cid1 orthologs in Arabidopsis thaliana, Caenorhabditis elegans and humans display PUP activity either in vitro or in Xenopus laevis oocytes. Here, we review the literature on Cid1, other PUPs and uridylation, a conserved and previously under-appreciated mechanism of RNA regulation.

Original publication

DOI

10.1016/j.bbagrm.2008.03.003

Type

Journal article

Journal

Biochim Biophys Acta

Publication Date

04/2008

Volume

1779

Pages

286 - 294

Keywords

Actins, Animals, Arabidopsis, Arabidopsis Proteins, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Cycle Proteins, Nucleotidyltransferases, Poly U, RNA, Fungal, RNA, Helminth, RNA, Plant, S Phase, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid, Xenopus Proteins, Xenopus laevis