Mammalian GLD-2 homologs are poly(A) polymerases

Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4407-12. doi: 10.1073/pnas.0400779101.

Jae Eun Kwak ¹, Liaoteng Wang, Scott Ballantyne, Judith Kimble, Marvin Wickens

Affiliations

Affiliation

1 Department of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, WI 53706-1544, USA.

PMID: 15070731 DOI: 10.1073/pnas.0400779101

Abstract

GLD-2 is a cytoplasmic poly(A) polymerase present in the Caenorhabditis elegans germ line and embryo. It is a divergent member of the DNA Polymerase beta nucleotidyl transferase superfamily, which includes CCA-adding Enzymes, DNA polymerases and eukaryotic nuclear poly(A) polymerases. The polyadenylation activity of GLD-2 is stimulated by physical interaction with an RNA binding protein, GLD-3. To test whether GLD-3 might stimulate GLD-2 by recruiting it to RNA, we tethered C. elegans GLD-2 to mRNAs in Xenopus oocytes by using MS2 coat protein. Tethered GLD-2 adds poly(A) and stimulates translation of the mRNA, demonstrating that recruitment is sufficient to stimulate polyadenylation activity. We use the same tethered assay to identify human and mouse poly(A) polymerases related to GLD-2. This may provide entrees to previously uncharacterized modes of polyadenylation in mammalian cells.

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