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• W2110388212 abstract "Abstract Background The Male Specific Lethal (MSL) complex is enriched on the single X chromosome in male Drosophila cells and functions to upregulate X-linked gene expression and equalize X-linked gene dosage with XX females. The zinc finger protein Zn72D is required for productive splicing of the maleless ( mle ) transcript, which encodes an essential subunit of the MSL complex. In the absence of Zn72D, MLE levels are decreased, and as a result, the MSL complex no longer localizes to the X chromosome and dosage compensation is disrupted. To understand the molecular basis of Zn72D function, we identified proteins that interact with Zn72D. Results Among several proteins that associate with Zn72D, we found the DEAD box helicase Belle (Bel). Simultaneous knockdown of Zn72D and bel restored MSL complex localization to the X chromosome and dosage compensation. MLE protein was restored to 70% of wild-type levels, although the level of productively spliced mle transcript was still four-fold lower than in wild-type cells. The increase in production of MLE protein relative to the amount of correctly spliced mle mRNA could not be attributed to an alteration in MLE stability. Conclusion These data indicate that Zn72D and Bel work together to control mle splicing and protein levels. Thus Zn72D and Bel may be factors that coordinate splicing and translational regulation." @default.
• W2110388212 created "2016-06-24" @default.
• W2110388212 creator A5044149769 @default.
• W2110388212 creator A5047663657 @default.
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• W2110388212 date "2009-04-22" @default.
• W2110388212 modified "2023-09-27" @default.
• W2110388212 title "The zinc finger protein Zn72D and DEAD box helicase Belle interact and control maleless mRNA and protein levels" @default.
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• W2110388212 doi "https://doi.org/10.1186/1471-2199-10-33" @default.
• W2110388212 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2680859" @default.
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