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2y0m

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Revision as of 07:43, 24 December 2014

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MOF

Structural highlights

2y0m is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:	,
Related:	2y0n
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MYST1_HUMAN] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The male-specific lethal (MSL) complex is required for dosage compensation in Drosophila melanogaster, and analogous complexes exist in mammals. We report structures of binary complexes of mammalian MSL3 and the histone acetyltransferase (HAT) MOF with consecutive segments of MSL1. MSL1 interacts with MSL3 as an extended chain forming an extensive hydrophobic interface, whereas the MSL1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of MSL1. This structure provides insights into the catalytic mechanism of MOF and enables us to show analogous interactions of MOF with NSL1. In Drosophila, selective disruption of Msl1 interactions with Msl3 or Mof severely affects Msl1 targeting to the body of dosage-compensated genes and several high-affinity sites, without affecting promoter binding. We propose that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting to the X chromosome.

Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1.,Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A Nat Struct Mol Biol. 2011 Feb;18(2):142-9. Epub 2011 Jan 9. PMID:21217699^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM. MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. J Biol Chem. 2002 Dec 27;277(52):50860-6. Epub 2002 Oct 22. PMID:12397079 doi:10.1074/jbc.M203839200
↑ Gupta A, Sharma GG, Young CS, Agarwal M, Smith ER, Paull TT, Lucchesi JC, Khanna KK, Ludwig T, Pandita TK. Involvement of human MOF in ATM function. Mol Cell Biol. 2005 Jun;25(12):5292-305. PMID:15923642 doi:25/12/5292
↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
↑ Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A. Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol. 2011 Feb;18(2):142-9. Epub 2011 Jan 9. PMID:21217699 doi:10.1038/nsmb.1960

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y0m"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y0m RCSB], [http://www.ebi.ac.uk/pdbsum/2y0m PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MYST1_HUMAN MYST1_HUMAN]] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.<ref>PMID:12397079</ref> <ref>PMID:15923642</ref> <ref>PMID:20018852</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 [[Category: Homo sapiens]]
 [[Category: Mus musculus]]
-[[Category: Akhtar, A.]]
+[[Category: Akhtar, A]]
-[[Category: Cusack, S.]]
+[[Category: Cusack, S]]
-[[Category: Hallacli, E.]]
+[[Category: Hallacli, E]]
-[[Category: Holz, H.]]
+[[Category: Holz, H]]
-[[Category: Kadlec, J.]]
+[[Category: Kadlec, J]]
-[[Category: Lipp, M.]]
+[[Category: Lipp, M]]
-[[Category: Weatherby, J Sanchez.]]
+[[Category: Weatherby, J Sanchez]]
 [[Category: Chromatin]]
 [[Category: Msl complex]]
 [[Category: Transcription]]
 [[Category: X chromosome]]

2y0m

From Proteopedia

Revision as of 07:43, 24 December 2014

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MOF

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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