The Library
Stimulation of translation by human Unr requires cold shock domains 2 and 4, and correlates with poly(A) binding protein interaction
Tools
Tools
Tools
Ray, Swagat and Anderson, Emma C. (2016) Stimulation of translation by human Unr requires cold shock domains 2 and 4, and correlates with poly(A) binding protein interaction. Scientific Reports, 6 . 22461. doi:10.1038/srep22461
|
PDF
WRAP_0673452-lf-040316-srep22461_published.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2266Kb) | Preview |
Official URL: http://dx.doi.org/10.1038/srep22461
Abstract
The RNA binding protein Unr, which contains five cold shock domains, has several specific roles in post-transcriptional control of gene expression. It can act as an activator or inhibitor of translation initiation, promote mRNA turnover, or stabilise mRNA. Its role depends on the mRNA and other proteins to which it binds, which includes cytoplasmic poly(A) binding protein 1 (PABP1). Since PABP1 binds to all polyadenylated mRNAs, and is involved in translation initiation by interaction with eukaryotic translation initiation factor 4G (eIF4G), we investigated whether Unr has a general role in translational control. We found that Unr strongly stimulates translation in vitro, and mutation of cold shock domains 2 or 4 inhibited its translation activity. The ability of Unr and its mutants to stimulate translation correlated with its ability to bind RNA, and to interact with PABP1. We found that Unr stimulated the binding of PABP1 to mRNA, and that Unr was required for the stable interaction of PABP1 and eIF4G in cells. siRNA-mediated knockdown of Unr reduced the overall level of cellular translation in cells, as well as that of cap-dependent and IRES-dependent reporters. These data describe a novel role for Unr in regulating cellular gene expression.
| Item Type: | Journal Article | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QH Natural history > QH426 Genetics Q Science > QR Microbiology |
||||||||
| Divisions: | Faculty of Science > Life Sciences (2010- ) | ||||||||
| Library of Congress Subject Headings (LCSH): | RNA-protein interactions, Gene expression, Messenger RNA, Protein binding | ||||||||
| Journal or Publication Title: | Scientific Reports | ||||||||
| Publisher: | Nature Publishing Group | ||||||||
| ISSN: | 2045-2322 | ||||||||
| Official Date: | 3 March 2016 | ||||||||
| Dates: |
|
||||||||
| Volume: | 6 | ||||||||
| Article Number: | 22461 | ||||||||
| DOI: | 10.1038/srep22461 | ||||||||
| Status: | Peer Reviewed | ||||||||
| Publication Status: | Published | ||||||||
| Access rights to Published version: | Open Access | ||||||||
| Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||||||
| Grant number: | BB/J001791/1 | ||||||||
| Adapted As: |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
