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Gene Review

mof  -  males absent on the first

Drosophila melanogaster

Synonyms: CG3025, Dmel\CG3025, Histone acetyl transferase MOF, MOF, Males-absent on the first protein, ...
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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


Regulatory relationships of mof


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].


  1. Chromodomains are protein-RNA interaction modules. Akhtar, A., Zink, D., Becker, P.B. Nature (2000) [Pubmed]
  2. Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. Akhtar, A., Becker, P.B. Mol. Cell (2000) [Pubmed]
  3. Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster. Gu, W., Szauter, P., Lucchesi, J.C. Dev. Genet. (1998) [Pubmed]
  4. Evolution of dosage compensation in Diptera: the gene maleless implements dosage compensation in Drosophila (Brachycera suborder) but its homolog in Sciara (Nematocera suborder) appears to play no role in dosage compensation. Ruiz, M.F., Esteban, M.R., Doñoro, C., Goday, C., Sánchez, L. Genetics (2000) [Pubmed]
  5. DNA supercoiling factor contributes to dosage compensation in Drosophila. Furuhashi, H., Nakajima, M., Hirose, S. Development (2006) [Pubmed]
  6. The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcription regulation. Eisen, A., Utley, R.T., Nourani, A., Allard, S., Schmidt, P., Lane, W.S., Lucchesi, J.C., Cote, J. J. Biol. Chem. (2001) [Pubmed]
  7. MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation complex. Buscaino, A., Köcher, T., Kind, J.H., Holz, H., Taipale, M., Wagner, K., Wilm, M., Akhtar, A. Mol. Cell (2003) [Pubmed]
  8. The MRG domain mediates the functional integration of MSL3 into the dosage compensation complex. Morales, V., Regnard, C., Izzo, A., Vetter, I., Becker, P.B. Mol. Cell. Biol. (2005) [Pubmed]
  9. Evolution of chromatin-remodeling complexes: comparative genomics reveals the ancient origin of "novel" compensasome genes. Marín, I. J. Mol. Evol. (2003) [Pubmed]
  10. Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3. Zhang, P., Du, J., Sun, B., Dong, X., Xu, G., Zhou, J., Huang, Q., Liu, Q., Hao, Q., Ding, J. Nucleic Acids Res. (2006) [Pubmed]
  11. Dosage dependent gene regulation and the compensation of the X chromosome in Drosophila males. Birchler, J.A., Pal-Bhadra, M., Bhadra, U. Genetica (2003) [Pubmed]
  12. Targeting the chromatin-remodeling MSL complex of Drosophila to its sites of action on the X chromosome requires both acetyl transferase and ATPase activities. Gu, W., Wei, X., Pannuti, A., Lucchesi, J.C. EMBO J. (2000) [Pubmed]
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