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Updated: Jul 6, 2026

Protocols for C-Brick DNA Standard Assembly Using Cpf1

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Published on: June 15, 2017

The Cid1 poly(U) polymerase.

Olivia S Rissland¹, Chris J Norbury

¹Sir William Dunn School of Pathology, University of Oxford, UK.

Biochimica Et Biophysica Acta

|March 29, 2008

Summary

The cytoplasmic protein Cid1 functions as a poly(U) polymerase (PUP), uridylating actin mRNA during S phase arrest. This RNA uridylation mechanism is conserved across species, highlighting its importance in gene regulation.

Area of Science:

Molecular Biology
RNA Biology
Biochemistry

Background:

The Schizosaccharomyces pombe cytoplasmic protein Cid1 is identified as a poly(U) polymerase (PUP).
Polyadenylated actin mRNA is a known target, undergoing uridylation during S phase arrest.
This suggests a broader role for Cid1 in regulating multiple RNA targets.

Purpose of the Study:

To review the literature on Cid1, other poly(U) polymerases (PUPs), and RNA uridylation.
To highlight RNA uridylation as a conserved and under-appreciated mechanism of RNA regulation.

Main Methods:

Literature review of studies on Cid1, PUPs, and uridylation.
Analysis of experimental data from in vitro assays and Xenopus laevis oocytes.

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Main Results:

Cid1 exhibits poly(U) polymerase activity, specifically uridylating actin mRNA.
Orthologs of Cid1 in Arabidopsis thaliana, Caenorhabditis elegans, and humans also demonstrate PUP activity.
RNA uridylation is a conserved biological process across diverse organisms.

Conclusions:

RNA uridylation mediated by poly(U) polymerases like Cid1 is a significant regulatory mechanism.
The conserved nature of this pathway underscores its fundamental importance in cellular processes.
Further research into uridylation is warranted to fully understand its role in gene expression.