ArticleRNA (New York, N.Y.)2008
Functional domains of Drosophila UNR in translational control.
Article in RNA (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras.Cell reports · 2020Article
- CSDE1 controls gene expression through the miRNA-mediated decay machinery.Life science alliance · 2020Article
- Article
- RNA Binding Proteins and Regulation of mRNA Translation in Erythropoiesis.Frontiers in physiology · 2018Review
- Promiscuity in post-transcriptional control of gene expression: Drosophila sex-lethal and its regulatory partnerships.FEBS letters · 2017Review
- Computational characterization of Iron metabolism in the Tsetse disease vector, Glossina morsitans: IRE stem-loops.BMC genomics · 2016Article
- Stimulation of translation by human Unr requires cold shock domains 2 and 4, and correlates with poly(A) binding protein interaction.Scientific reports · 2016Article
- Article
- Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex.Journal of biomolecular NMR · 2013Article
- Before It Gets Started: Regulating Translation at the 5' UTR.Comparative and functional genomics · 2012Article
- Widespread generation of alternative UTRs contributes to sex-specific RNA binding by UNR.RNA (New York, N.Y.) · 2012Article
- The translation initiation factor eIF4E regulates the sex-specific expression of the master switch gene Sxl in Drosophila melanogaster.PLoS genetics · 2011Article
- Computational annotation of UTR cis-regulatory modules through Frequent Pattern Mining.BMC bioinformatics · 2009Article
- Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites.Cell cycle (Georgetown, Tex.) · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translational repression of male-specific-lethal 2 (msl-2) mRNA by Sex-lethal (SXL) is an essential regulatory step of X chromosome dosage compensation in Drosophila. Translation inhibition requires that SXL recruits the protein upstream of N-ras (UNR) to the 3' UTR of msl-2 mRNA. UNR is a conserved, ubiquitous protein that contains five cold-shock domains (CSDs). Here, we dissect the domains of UNR required for translational repression and complex formation with SXL and msl-2 mRNA. Using gel-mobility shift assays, the domain involved in interactions with SXL and msl-2 was mapped specifically to the first CSD (CSD1). Indeed, excess of a peptide containing this domain derepressed msl-2 translation in vitro. The CSD1 of human UNR can also form a complex with SXL and msl-2. Comparative analyses of the CSDs of the Drosophila and human proteins together with site-directed mutagenesis experiments revealed that three exposed residues within CSD1 are required for complex formation. Tethering assays showed that CSD1 is not sufficient for translational repression, indicating that UNR binding to SXL and msl-2 can be distinguished from translation inhibition. Repression by tethered UNR requires residues from both the amino-terminal Q-rich stretch and the two first CSDs, indicating that the translational effector domain of UNR resides within the first 397 amino acids of the protein. Our results identify domains and residues required for UNR function in translational control.
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