Moschall, Rebecca and Strauss, Daniela and Garcia-Beyaert, Marina and Gebauer, Fatima and Medenbach, Jan (2018) Drosophila Sister-of-Sex-lethal is a repressor of translation. RNA, 24 (2). pp. 149-158. ISSN 1355-8382, 1469-9001
Full text not available from this repository. (Request a copy)Abstract
The RNA-binding protein Sex-lethal (Sxl) is an important post-transcriptional regulator of sex determination and dosage compensation in female Drosophila. To prevent the assembly of the MSL dosage compensation complex in female flies, Sxl acts as a repressor of male-specific lethal-2 (msl-2) mRNA translation. It uses two distinct and mutually reinforcing blocks to translation that operate on the 5' and 3' untranslated regions (UTRs) of msl-2 mRNA, respectively. While 5' UTR-mediated translational control involves an upstream open reading frame, 3' UTR-mediated regulation strictly requires the co-repressor protein Upstream of N-ras (Unr), which is recruited to the transcript by Sxl. We have identified the protein Sister-of-Sex-lethal (Ssx) as a novel repressor of translation with Sxl-like activity. Both proteins have a comparable RNA-binding specificity and can associate with uracil-rich RNA regulatory elements present in msl-2 mRNA. Moreover, both repress translation when bound to the 5' UTR of msl-2. However, Ssx is inactive in 3' UTR-mediated regulation, as it cannot engage the co-repressor protein Unr. The difference in activity maps to the first RNA-recognition motif (RRM) of Ssx. Conversion of three amino acids within this domain into their Sxl counterpart results in a gain of function and repression via the 3' UTR, allowing detailed insights into the evolutionary origin of the two proteins and into the molecular requirements of an important translation regulatory pathway.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MSL-2 MESSENGER-RNA; DOSAGE COMPENSATION; DETERMINING GENE; STRUCTURAL BASIS; PROTEIN; UNR; MECHANISM; SXL; INSECTS; MELANOGASTER; regulation of translation; Sex-lethal; male-specific lethal-2; protein evolution |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 20 Mar 2020 14:13 |
| Last Modified: | 20 Mar 2020 14:13 |
| URI: | https://pred.uni-regensburg.de/id/eprint/15161 |
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