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Molecular and Cellular Biology, May 2007, p. 3612-3624, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02209-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Efficient RNA Polyuridylation by Noncanonical Poly(A) Polymerases{triangledown} ,{dagger}

Olivia S. Rissland, Andrea Mikulasova, and Chris J. Norbury*

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

Received 25 November 2006/ Returned for modification 2 January 2007/ Accepted 5 March 2007

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.

* Corresponding author. Mailing address: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom. Phone: 44 1865 275 540. Fax: 44 1865 275 501. E-mail: chris.norbury{at}path.ox.ac.uk

{triangledown} Published ahead of print on 12 March 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, May 2007, p. 3612-3624, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02209-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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