About MORF4L / Mortality Factor:
Component of the NuA4 histone acetyltransferase (HAT) complex, which is involved in the transcriptional activation of specific genes primarily through the acetylation of nucleosomal histones H4 and H2A. This modification may affect nucleosome-DNA interactions and the interaction of the modified histones with other proteins that positively regulate transcription.
This complex may be necessary to activate transcriptional programs involved in oncogene and proto-oncogene-mediated growth induction, tumor suppressor-mediated growth arrest and replicative senescence, apoptosis, and DNA repair. When NuA4 is recruited to sites of DNA damage, it may also play a direct role in DNA repair.
Component of the NuA4 histone acetyltransferase complex, which also includes the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GA MYC, and the adenovirus E1A protein interact with the NuA4 complex. MRGBP may have direct interactions with MORF4L1/MRG15 and MORF4L2/MRGX.
As a result, common MORF functions are most likely elicited by a MORF/mSin3A/TLE complex action. While the MORFs may have similar functions, MRG15 interacts with Pf1 but not MRGX or MORF4. As a result, MRG15 may have functions distinct from MRGX and MORF4. Pf1 reduced transcriptional repression by Gal4-MRG15 but did not affect repression by MRGX or MORF4. MRG15 and mSin3A have separate binding sites on Pf1. Furthermore, Pf1 and MRG15 bind to different domains on mSin3A. These findings suggest that the unique functions of MRG15 are elicited by an MRG15/Pf1/mSin3A complex.