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| - | [[Image:2bud.gif|left|200px]]<br /><applet load="2bud" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="2bud" /> | |
| - | '''THE SOLUTION STRUCTURE OF THE CHROMO BARREL DOMAIN FROM THE MALES-ABSENT ON THE FIRST (MOF) PROTEIN'''<br /> | |
| | | | |
| - | ==Overview== | + | ==The solution structure of the chromo barrel domain from the males- absent on the first (MOF) protein== |
| - | 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. | + | <StructureSection load='2bud' size='340' side='right'caption='[[2bud]]' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[2bud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUD FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bud OCA], [https://pdbe.org/2bud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bud RCSB], [https://www.ebi.ac.uk/pdbsum/2bud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bud ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MOF_DROME 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).<ref>PMID:11258702</ref> <ref>PMID:16543150</ref> <ref>PMID:20620954</ref> <ref>PMID:34133927</ref> <ref>PMID:9155031</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bud_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bud ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == 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. |
| | | | |
| - | ==About this 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<ref>PMID:15964847</ref> |
| - | 2BUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUD OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15964847 15964847]
| + | </div> |
| | + | <div class="pdbe-citations 2bud" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
| - | [[Category: Histone acetyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Single protein]]
| + | [[Category: Akhtar A]] |
| - | [[Category: Akhtar, A.]] | + | [[Category: Buscaino A]] |
| - | [[Category: Buscaino, A.]] | + | [[Category: Laue ED]] |
| - | [[Category: Laue, E.D.]] | + | [[Category: Murzin AG]] |
| - | [[Category: Murzin, A.G.]] | + | [[Category: Murzina NV]] |
| - | [[Category: Murzina, N.V.]] | + | [[Category: Nielsen PR]] |
| - | [[Category: Nielsen, P.R.]] | + | [[Category: Nietlispach D]] |
| - | [[Category: Nietlispach, D.]] | + | [[Category: Warner RJ]] |
| - | [[Category: Warner, R.J.]] | + | |
| - | [[Category: acetyl-transfer]]
| + | |
| - | [[Category: beta barrel]]
| + | |
| - | [[Category: chromodomain like]]
| + | |
| - | [[Category: dcc]]
| + | |
| - | [[Category: dosage compensation complex]]
| + | |
| - | [[Category: hat]]
| + | |
| - | [[Category: metal-binding]]
| + | |
| - | [[Category: mof]]
| + | |
| - | [[Category: royal family]]
| + | |
| - | [[Category: transferase acyltransferase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:55:26 2007''
| + | |
| 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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