2jmj

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[[Image:2jmj.jpg|left|200px]]
[[Image:2jmj.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2jmj |SIZE=350|CAPTION= <scene name='initialview01'>2jmj</scene>
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The line below this paragraph, containing "STRUCTURE_2jmj", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= YNG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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{{STRUCTURE_2jmj| PDB=2jmj | SCENE= }}
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|RELATEDENTRY=[[2jmi|2JMI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmj OCA], [http://www.ebi.ac.uk/pdbsum/2jmj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jmj RCSB]</span>
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}}
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'''NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide'''
'''NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide'''
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[[Category: Tanny, J C.]]
[[Category: Tanny, J C.]]
[[Category: Taverna, S D.]]
[[Category: Taverna, S D.]]
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[[Category: complex]]
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[[Category: Complex]]
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[[Category: h3k4me3]]
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[[Category: H3k4me3]]
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[[Category: histone]]
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[[Category: Histone]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: phd]]
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[[Category: Phd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:02:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:59:18 2008''
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Revision as of 06:02, 4 May 2008

Template:STRUCTURE 2jmj

NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide


Overview

Posttranslational histone modifications participate in modulating the structure and function of chromatin. Promoters of transcribed genes are enriched with K4 trimethylation and hyperacetylation on the N-terminal tail of histone H3. Recently, PHD finger proteins, like Yng1 in the NuA3 HAT complex, were shown to interact with H3K4me3, indicating a biochemical link between K4 methylation and hyperacetylation. By using a combination of mass spectrometry, biochemistry, and NMR, we detail the Yng1 PHD-H3K4me3 interaction and the importance of NuA3-dependent acetylation at K14. Furthermore, genome-wide ChIP-Chip analysis demonstrates colocalization of Yng1 and H3K4me3 in vivo. Disrupting the K4me3 binding of Yng1 altered K14ac and transcription at certain genes, thereby demonstrating direct in vivo evidence of sequential trimethyl binding, acetyltransferase activity, and gene regulation by NuA3. Our data support a general mechanism of transcriptional control through which histone acetylation upstream of gene activation is promoted partially through availability of H3K4me3, "read" by binding modules in select subunits.

About this Structure

2JMJ is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs., Taverna SD, Ilin S, Rogers RS, Tanny JC, Lavender H, Li H, Baker L, Boyle J, Blair LP, Chait BT, Patel DJ, Aitchison JD, Tackett AJ, Allis CD, Mol Cell. 2006 Dec 8;24(5):785-96. PMID:17157260 Page seeded by OCA on Sun May 4 09:02:04 2008

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