6qxz

From Proteopedia

(Difference between revisions)

Revision as of 12:44, 16 December 2020

Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4

Structural highlights

6qxz is a 2 chain structure with sequence from Arath. This structure supersedes the now removed PDB entry 6hbo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	ASHH2, EFS, LAZ2, SDG8, SET8, At1g77300, T14N5.15 (ARATH)
Activity:	Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASHH2_ARATH] Histone methyltransferase involved in di and tri-methylation of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3). Binds to H3 already mono- or di-methylated on 'Lys-4'(H3K4me1 or H3K4me2), but not to H3K4me3. H3K4me and H3K36me represent specific tags for epigenetic transcriptional activation. Regulates positively FLC transcription to prevent early flowering transition. Required for flowering transition in response to vernalization and for the maintenance of FLC expression in late embryos, but dispensable for the initial reactivation in early embryos during reprogramming. Seems also to modulate several traits including floral organ size, root size and dormancy. Promotes apical dominance (PubMed:16299497, PubMed:10518493, PubMed:16258034, PubMed:18070919, PubMed:19915673, PubMed:20711170). Directly involved in the tri-methylation of 'Lys-36' of histone H3 (H3K36me3) at LAZ5 chromatin to maintain a transcriptionally active state of LAZ5, a TIR-NB-LRR protein involved in innate immunity (PubMed:20949080).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

The ASHH2 CW domain is responsible for recognizing the methylation state at lysine 4 of histone 3 N-terminal tails and implicated in the recruitment of the ASHH2 methyltransferase enzyme correctly to the histones. The ASHH2 CW domain binds H3 lysine motifs that can be either mono-, di-, or tri-methylated [ARTK(meX)QTAR, where X denotes the number of methylations], but binds strongest to monomethylated instances (Kd values reported in the range of 1 microm to 500 nM). Hoppmann et al. published the uncomplexed NMR structure of an ASHH2 CW domain in 2011. Here we document the assignment of a shortened ASHH2 CW construct, CW42, with similar binding affinity and better expression yields than the one used to solve the uncomplexed structure. We also perform (1)H-(15)N HSQC-monitored titrations that document at which protein-peptide ratios the complex is saturated. Backbone resonance assignments are presented for this shortened ASHH2 CW domain alone and bound to an H3 histone tail mimicking peptide monomethylated on lysine 4 (ARTK(me1)QTAR). Likewise, the assignment was also performed for the protein in complex with the dimethylated (ARTK(me2)QTAR) and trimethylated (ARTK(me3)QTAR) peptide. Overall, these two latter situations displayed a similar perturbation of shifts as the mono-methylated instance. In the case of the monomethylated histone tail mimic, side-chain assignment of CW42 in this complex was performed and reported in addition to backbone assignment, in preparation of a future solution structure determination and dynamics characterization of the CW42-ARTK(me1)QTAR complex.

(1)H, (13)C, and (15)N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides.,Dobrovolska O, Bril'kov M, Odegard-Fougner O, Aasland R, Halskau O Biomol NMR Assign. 2018 Apr;12(1):215-220. doi: 10.1007/s12104-018-9811-x. Epub, 2018 Feb 16. PMID:29453713^[8]

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

References

↑ Soppe WJ, Bentsink L, Koornneef M. The early-flowering mutant efs is involved in the autonomous promotion pathway of Arabidopsis thaliana. Development. 1999 Nov;126(21):4763-70. PMID:10518493
↑ Kim SY, He Y, Jacob Y, Noh YS, Michaels S, Amasino R. Establishment of the vernalization-responsive, winter-annual habit in Arabidopsis requires a putative histone H3 methyl transferase. Plant Cell. 2005 Dec;17(12):3301-10. Epub 2005 Oct 28. PMID:16258034 doi:http://dx.doi.org/10.1105/tpc.105.034645
↑ Zhao Z, Yu Y, Meyer D, Wu C, Shen WH. Prevention of early flowering by expression of FLOWERING LOCUS C requires methylation of histone H3 K36. Nat Cell Biol. 2005 Dec;7(12):1256-60. Epub 2005 Nov 20. PMID:16299497 doi:http://dx.doi.org/10.1038/ncb1329
↑ Xu L, Zhao Z, Dong A, Soubigou-Taconnat L, Renou JP, Steinmetz A, Shen WH. Di- and tri- but not monomethylation on histone H3 lysine 36 marks active transcription of genes involved in flowering time regulation and other processes in Arabidopsis thaliana. Mol Cell Biol. 2008 Feb;28(4):1348-60. Epub 2007 Dec 10. PMID:18070919 doi:http://dx.doi.org/10.1128/MCB.01607-07
↑ Grini PE, Thorstensen T, Alm V, Vizcay-Barrena G, Windju SS, Jorstad TS, Wilson ZA, Aalen RB. The ASH1 HOMOLOG 2 (ASHH2) histone H3 methyltransferase is required for ovule and anther development in Arabidopsis. PLoS One. 2009 Nov 12;4(11):e7817. doi: 10.1371/journal.pone.0007817. PMID:19915673 doi:http://dx.doi.org/10.1371/journal.pone.0007817
↑ Ko JH, Mitina I, Tamada Y, Hyun Y, Choi Y, Amasino RM, Noh B, Noh YS. Growth habit determination by the balance of histone methylation activities in Arabidopsis. EMBO J. 2010 Sep 15;29(18):3208-15. doi: 10.1038/emboj.2010.198. Epub 2010 Aug, 13. PMID:20711170 doi:http://dx.doi.org/10.1038/emboj.2010.198
↑ Palma K, Thorgrimsen S, Malinovsky FG, Fiil BK, Nielsen HB, Brodersen P, Hofius D, Petersen M, Mundy J. Autoimmunity in Arabidopsis acd11 is mediated by epigenetic regulation of an immune receptor. PLoS Pathog. 2010 Oct 7;6(10):e1001137. doi: 10.1371/journal.ppat.1001137. PMID:20949080 doi:http://dx.doi.org/10.1371/journal.ppat.1001137
↑ Dobrovolska O, Bril'kov M, Odegard-Fougner O, Aasland R, Halskau O. (1)H, (13)C, and (15)N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides. Biomol NMR Assign. 2018 Apr;12(1):215-220. doi: 10.1007/s12104-018-9811-x. Epub, 2018 Feb 16. PMID:29453713 doi:http://dx.doi.org/10.1007/s12104-018-9811-x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6qxz"

@@ Line 3: / Line 3: @@
 <StructureSection load='6qxz' size='340' side='right'caption='[[6qxz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6qxz]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6hbo 6hbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QXZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QXZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6qxz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6hbo 6hbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QXZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QXZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASHH2, EFS, LAZ2, SDG8, SET8, At1g77300, T14N5.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
-<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=6qxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qxz OCA], [http://pdbe.org/6qxz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qxz RCSB], [http://www.ebi.ac.uk/pdbsum/6qxz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qxz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qxz OCA], [http://pdbe.org/6qxz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qxz RCSB], [http://www.ebi.ac.uk/pdbsum/6qxz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qxz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 21: @@
 </div>
 <div class="pdbe-citations 6qxz" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone 3D structures|Histone 3D structures]]
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Arath]]
 [[Category: Histone-lysine N-methyltransferase]]
 [[Category: Large Structures]]

6qxz

From Proteopedia

Revision as of 12:44, 16 December 2020

Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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