2j8a: Difference between revisions

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<StructureSection load='2j8a' size='340' side='right'caption='[[2j8a]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='2j8a' size='340' side='right'caption='[[2j8a]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8A FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8A FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=2j8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8a OCA], [https://pdbe.org/2j8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8a RCSB], [https://www.ebi.ac.uk/pdbsum/2j8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8a ProSAT]</span></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=2j8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8a OCA], [https://pdbe.org/2j8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8a RCSB], [https://www.ebi.ac.uk/pdbsum/2j8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SET1_YEAST SET1_YEAST] Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11751634</ref> <ref>PMID:11752412</ref> <ref>PMID:11805083</ref> <ref>PMID:11818070</ref> <ref>PMID:12060701</ref> <ref>PMID:12353038</ref> <ref>PMID:12845608</ref> <ref>PMID:14636589</ref> <ref>PMID:15949446</ref> <ref>PMID:9398665</ref> <ref>PMID:9988274</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2j8a ConSurf].
</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=2j8a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, in addition to its catalytic SET domain, a conserved RNA recognition motif (RRM1). We present here the crystal structure and the secondary structure assignment in solution of the Set1 RRM1. Although RRM1 has the expected betaalphabetabetaalphabeta RRM-fold, it lacks the typical RNA-binding features of these modules. RRM1 is not able to bind RNA by itself in vitro, but a construct combining RRM1 with a newly identified downstream RRM2 specifically binds RNA. In vivo, H3K4 methylation is not affected by a point mutation in RRM2 that preserves Set1 stability but affects RNA binding in vitro. In contrast mutating RRM1 destabilizes Set1 and leads to an increase of dimethylation of H3K4 at the 5'-coding region of active genes at the expense of trimethylation, whereas both, dimethylation decreases at the 3'-coding region. Taken together, our results suggest that Set1 RRMs bind RNA, but Set1 RNA-binding activity is not linked to H3K4 methylation.
Structural characterization of Set1 RNA recognition motifs and their role in histone H3 lysine 4 methylation.,Tresaugues L, Dehe PM, Guerois R, Rodriguez-Gil A, Varlet I, Salah P, Pamblanco M, Luciano P, Quevillon-Cheruel S, Sollier J, Leulliot N, Couprie J, Tordera V, Zinn-Justin S, Chavez S, van Tilbeurgh H, Geli V J Mol Biol. 2006 Jun 23;359(5):1170-81. Epub 2006 May 9. PMID:16787775<ref>PMID:16787775</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2j8a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chavez, S]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Couprie, J]]
[[Category: Chavez S]]
[[Category: Dehe, P M]]
[[Category: Couprie J]]
[[Category: Geli, V]]
[[Category: Dehe PM]]
[[Category: Guerois, R]]
[[Category: Geli V]]
[[Category: Leulliot, N]]
[[Category: Guerois R]]
[[Category: Luciano, P]]
[[Category: Leulliot N]]
[[Category: Pamblanco, M]]
[[Category: Luciano P]]
[[Category: Quevillon-Cheruel, S]]
[[Category: Pamblanco M]]
[[Category: Rodriguez-Gil, A]]
[[Category: Quevillon-Cheruel S]]
[[Category: Salah, P]]
[[Category: Rodriguez-Gil A]]
[[Category: Sollier, J]]
[[Category: Salah P]]
[[Category: Tilbeurgh, H Van]]
[[Category: Sollier J]]
[[Category: Tordera, V]]
[[Category: Tordera V]]
[[Category: Tresaugues, L]]
[[Category: Tresaugues L]]
[[Category: Varlet, I]]
[[Category: Van Tilbeurgh H]]
[[Category: Zinn-Justin, S]]
[[Category: Varlet I]]
[[Category: Chromosomal protein]]
[[Category: Zinn-Justin S]]
[[Category: Histone methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Nuclear protein]]
[[Category: Rrm fold]]
[[Category: Telomere]]
[[Category: Transferase]]

Latest revision as of 12:35, 9 May 2024

X-ray structure of the N-terminus RRM domain of Set1X-ray structure of the N-terminus RRM domain of Set1

Structural highlights

2j8a is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SET1_YEAST Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
  2. ↑ Briggs SD, Bryk M, Strahl BD, Cheung WL, Davie JK, Dent SY, Winston F, Allis CD. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 2001 Dec 15;15(24):3286-95. doi: 10.1101/gad.940201. PMID:11751634 doi:http://dx.doi.org/10.1101/gad.940201
  3. ↑ Nagy PL, Griesenbeck J, Kornberg RD, Cleary ML. A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):90-4. Epub 2001 Dec 18. PMID:11752412 doi:http://dx.doi.org/10.1073/pnas.221596698
  4. ↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
  5. ↑ Bryk M, Briggs SD, Strahl BD, Curcio MJ, Allis CD, Winston F. Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism. Curr Biol. 2002 Jan 22;12(2):165-70. PMID:11818070
  6. ↑ Bernstein BE, Humphrey EL, Erlich RL, Schneider R, Bouman P, Liu JS, Kouzarides T, Schreiber SL. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8695-700. Epub 2002 Jun 11. PMID:12060701 doi:http://dx.doi.org/10.1073/pnas.082249499
  7. ↑ Santos-Rosa H, Schneider R, Bannister AJ, Sherriff J, Bernstein BE, Emre NC, Schreiber SL, Mellor J, Kouzarides T. Active genes are tri-methylated at K4 of histone H3. Nature. 2002 Sep 26;419(6905):407-11. Epub 2002 Sep 11. PMID:12353038 doi:http://dx.doi.org/10.1038/nature01080
  8. ↑ Boa S, Coert C, Patterton HG. Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression. Yeast. 2003 Jul 15;20(9):827-35. doi: 10.1002/yea.995. PMID:12845608 doi:http://dx.doi.org/10.1002/yea.995
  9. ↑ Santos-Rosa H, Schneider R, Bernstein BE, Karabetsou N, Morillon A, Weise C, Schreiber SL, Mellor J, Kouzarides T. Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin. Mol Cell. 2003 Nov;12(5):1325-32. doi: 10.1016/s1097-2765(03)00438-6. PMID:14636589 doi:http://dx.doi.org/10.1016/s1097-2765(03)00438-6
  10. ↑ Morillon A, Karabetsou N, Nair A, Mellor J. Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription. Mol Cell. 2005 Jun 10;18(6):723-34. PMID:15949446 doi:http://dx.doi.org/S1097-2765(05)01315-8
  11. ↑ Nislow C, Ray E, Pillus L. SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes. Mol Biol Cell. 1997 Dec;8(12):2421-36. doi: 10.1091/mbc.8.12.2421. PMID:9398665 doi:http://dx.doi.org/10.1091/mbc.8.12.2421
  12. ↑ Corda Y, Schramke V, Longhese MP, Smokvina T, Paciotti V, Brevet V, Gilson E, Geli V. Interaction between Set1p and checkpoint protein Mec3p in DNA repair and telomere functions. Nat Genet. 1999 Feb;21(2):204-8. PMID:9988274 doi:http://dx.doi.org/10.1038/5991

2j8a, resolution 3.00Å

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