High impact information on mof

• In vitro analyses of the MOF and MSL-3 chromodomains indicate that these chromodomains may function as RNA interaction modules [1].
• MOF specifically binds through its chromodomain to roX2 RNA in vivo [1].
• Dosage compensation is an epigenetic process involving the specific acetylation of histone H4 at lysine 16 by the histone acetyltransferase MOF [1].
• Here we show that association of MOF with the male X chromosome depends on its interaction with RNA [1].
• Acetylation of chromatin by MOF, therefore, appears to be causally involved in transcriptional activation during dosage compensation [2].

Biological context of mof

• Experimental results and sequence analysis suggest that the mof gene encodes an acetyl transferase that plays a direct role in the specific histone acetylation associated with dosage compensation [3].
• The affinity-purified antibodies against D. melanogaster MSL1, MSL3, and MOF proteins involved in dosage compensation also revealed no differences in the staining pattern between the X chromosome and the autosomes in both Sciara males and females [4].
• This phenotype was dependent on the histone acetyltransferase MOF and was suppressed by simultaneous overexpression of ISWI [5].
• A point mutation in the MOF acetyl-CoA-binding site results in male-specific lethality [6].
• Yeast Esa1p, a MOF homolog, is essential for cell cycle progression and is the catalytic subunit of the NuA4 acetyltransferase complex [6].

Associations of mof 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 [7].

Regulatory relationships of mof

• MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation complex [7].

Other interactions of mof

• We showed previously that MSL3 is essential for the activation of MOF's nucleosomal histone acetyltransferase activity within an MSL1-MOF complex [8].
• Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) have an ancient origin [9].
• The MRG15 chromo domain consists of a beta-barrel and a long alpha-helix and assumes a structure more similar to the Drosophila MOF chromo barrel domain than the typical HP1/Pc chromo domains [10].
• However, the MSL (male specific lethal) complex modifies this effect on the autosomes, which would otherwise double their expression, by becoming sequestered to the X chromosome together with a histone acetylase (MOF) and kinase (JIL1) [11].
• We have investigated the role that the enzymatic activities of two complex components, the histone acetyltransferase activity of MOF and the ATPase activity of MLE, may have in the targeting and association of the complex with the X chromosome [12].

References