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

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 restor

SUBMITTER: Worringer KA 

PROVIDER: S-EPMC2680859 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature