Apr 24, 2009

The zinc finger protein Zn72D and DEAD box helicase Belle interact and control maleless mRNA and protein levels

BMC Molecular Biology
Kathleen A WorringerBarbara Panning

Abstract

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. 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. These data indicate that Zn72D and Bel work together to control mle splicing and protein lev...Continue Reading

Mentioned in this Paper

Pathologic Cytolysis
Establishment and Maintenance of Localization
Zinc Fingers
Real-Time Polymerase Chain Reaction
Northern Blotting
AGO2 gene
RPS3 gene
Untranslated Regions
Glycerin
Gene Knockdown Techniques

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