Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-3725
Proc Natl Acad Sci U S A 2004 Mar 30;10113:4407-12. doi: 10.1073/pnas.0400779101.
Show Gene links Show Anatomy links

Mammalian GLD-2 homologs are poly(A) polymerases.

Kwak JE , Wang L , Ballantyne S , Kimble J , Wickens M .


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.

PubMed ID: 15070731
PMC ID: PMC384760
Article link: Proc Natl Acad Sci U S A
Grant support: [+]


References [+] :
Aravind, DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history. 1999, Pubmed