| Structural highlights
Function
MOF_DROME Histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation as part of the male-specific lethal (MSL) complex (PubMed:9155031, PubMed:16543150, PubMed:34133927). Dosage compensation insures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes (PubMed:9155031). May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males where it is recruited by the MSL complex (PubMed:11258702). As part of the nonspecific lethal (NLS) complex may associate with promoters of X chromosomal as well as autosomal genes and positively regulate their transcription through chromatin modification (PubMed:20620954).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.
Structure of the chromo barrel domain from the MOF acetyltransferase.,Nielsen PR, Nietlispach D, Buscaino A, Warner RJ, Akhtar A, Murzin AG, Murzina NV, Laue ED J Biol Chem. 2005 Sep 16;280(37):32326-31. Epub 2005 Jun 17. PMID:15964847[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Akhtar A, Becker PB. The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition. EMBO Rep. 2001 Feb;2(2):113-8. PMID:11258702 doi:10.1093/embo-reports/kve022
- ↑ Mendjan S, Taipale M, Kind J, Holz H, Gebhardt P, Schelder M, Vermeulen M, Buscaino A, Duncan K, Mueller J, Wilm M, Stunnenberg HG, Saumweber H, Akhtar A. Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol Cell. 2006 Mar 17;21(6):811-23. PMID:16543150 doi:10.1016/j.molcel.2006.02.007
- ↑ Raja SJ, Charapitsa I, Conrad T, Vaquerizas JM, Gebhardt P, Holz H, Kadlec J, Fraterman S, Luscombe NM, Akhtar A. The nonspecific lethal complex is a transcriptional regulator in Drosophila. Mol Cell. 2010 Jun 25;38(6):827-41. PMID:20620954 doi:10.1016/j.molcel.2010.05.021
- ↑ Aleman JR, Kuhn TM, Pascual-Garcia P, Gospocic J, Lan Y, Bonasio R, Little SC, Capelson M. Correct dosage of X chromosome transcription is controlled by a nuclear pore component. Cell Rep. 2021 Jun 15;35(11):109236. PMID:34133927 doi:10.1016/j.celrep.2021.109236
- ↑ Hilfiker A, Hilfiker-Kleiner D, Pannuti A, Lucchesi JC. mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J. 1997 Apr 15;16(8):2054-60. PMID:9155031 doi:10.1093/emboj/16.8.2054
- ↑ Nielsen PR, Nietlispach D, Buscaino A, Warner RJ, Akhtar A, Murzin AG, Murzina NV, Laue ED. Structure of the chromo barrel domain from the MOF acetyltransferase. J Biol Chem. 2005 Sep 16;280(37):32326-31. Epub 2005 Jun 17. PMID:15964847 doi:10.1074/jbc.M501347200
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