High impact information on msl-3

• In vitro analyses of the MOF and MSL-3 chromodomains indicate that these chromodomains may function as RNA interaction modules [1].
• We find that the acetylation status of MSL-3 determines its interaction with roX2 RNA [2].
• We observe that localization of MSL-3 to the X chromosome is RNA dependent and acetylation sensitive [2].
• MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation complex [2].
• Mutagenesis of evolutionarily conserved sequences diminishes MSL binding in vivo [3].

Biological context of msl-3

• We have found that MSL-3 is also associated with the male X chromosome [4].
• Simultaneous contact of MOF with MSL1 and MSL3 led to its recruitment to chromatin, a dramatic stimulation of HAT activity and to improved substrate specificity [5].
• Our results demonstrate that MSL-3 localization to the male X chromosome and transcriptional upregulation of X-linked genes are two separable functions of the MSL-3 protein [6].
• Here, we show that MSL-3 is essential for cell viability and that three domains in the protein have distinct roles in dosage compensation [6].
• The polar region cooperates with the CBD in MSL-3 function, whereas the MRG domain is responsible for targeting the protein to the X chromosome [6].

Associations of msl-3 with chemical compounds

• We show that interaction of MOF with MSL-3 leads to specific acetylation of MSL-3 at a single lysine residue adjacent to one of its chromodomains [2].
• Other proteins belonging to the family include estrogen-induced gene 2 and the ethanol-induced 6 protein [7].

Regulatory relationships of msl-3

• We have further investigated whether Sxl negatively regulates MSL-3 X-chromosome binding in females and whether MSL-3 X-chromosome binding requires the other msls [4].

Other interactions of msl-3

• We found that MSL-2 binds in a reproducible, partial pattern to the male X chromosome in the absence of MLE or MSL-3, or when ectopically expressed at a low level in females [8].
• Interaction with MSL1 mediates the activation of MOF in vitro and the targeting of MSL3 to the X-chromosomal territory in vivo [9].
• By characterizing the MSL3 domain structure and its associated functions, we now found that the nucleic acid binding determinants reside in the N terminus of MSL3, well separable from the C-terminal MRG signatures that form an integrated domain required for MSL1 interaction [9].
• These analyses also suggest that the msl-3/MRG15 duplication occurred after the fungus/animal split, while an independent duplication occurred in plants [10].

References