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PMID:16452508
Citation |
Duncan, K, Grskovic, M, Strein, C, Beckmann, K, Niggeweg, R, Abaza, I, Gebauer, F, Wilm, M and Hentze, MW (2006) Sex-lethal imparts a sex-specific function to UNR by recruiting it to the msl-2 mRNA 3' UTR: translational repression for dosage compensation. Genes Dev. 20:368-79 |
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Abstract |
MSL-2 (male-specific lethal 2) is the limiting component of the Drosophila dosage compensation complex (DCC) that specifically increases transcription from the male X chromosome. Ectopic expression of MSL-2 protein in females causes DCC assembly on both X chromosomes and lethality. Inhibition of MSL-2 synthesis requires the female-specific protein sex-lethal (SXL), which binds to the msl-2 mRNA 5' and 3' untranslated regions (UTRs) and blocks translation through distinct UTR-specific mechanisms. Here, we purify translationally silenced msl-2 mRNPs and identify UNR (upstream of N-ras) as a protein recruited to the 3' UTR by SXL. We demonstrate that SXL requires UNR as a corepressor for 3'-UTR-mediated regulation, imparting a female-specific function to the ubiquitously expressed UNR protein. Our results reveal a novel functional role for UNR as a translational repressor and indicate that UNR is a key component of a "fail-safe" dosage compensation regulatory system that prevents toxic MSL-2 synthesis in female cells. |
Links |
PubMed PMC1361707 Online version:10.1101/gad.371406 |
Keywords |
3' Untranslated Regions/genetics; 3' Untranslated Regions/metabolism; Amino Acid Sequence; Animals; Cytoplasm/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; DNA-Binding Proteins/physiology; Dosage Compensation, Genetic; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Drosophila Proteins/physiology; Female; Humans; Male; Models, Biological; Models, Genetic; Molecular Sequence Data; Nuclear Proteins/genetics; Nuclear Proteins/metabolism; Protein Biosynthesis/genetics; Protein Biosynthesis/physiology; RNA, Messenger/genetics; RNA, Messenger/metabolism; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Ribonucleoproteins/genetics; Ribonucleoproteins/metabolism; Sequence Homology; Transcription Factors/genetics; Transcription Factors/metabolism; Transfection |
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