2JMI
NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state
Summary for 2JMI
| Entry DOI | 10.2210/pdb2jmi/pdb |
| Related | 2JMJ |
| Descriptor | Protein YNG1, ZINC ION (2 entities in total) |
| Functional Keywords | phd, histone, recognition, yeast, protein binding |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: Q08465 |
| Total number of polymer chains | 1 |
| Total formula weight | 10400.46 |
| Authors | Ilin, S.,Taverna, S.D.,Rogers, R.S.,Tanny, J.C.,Lavender, H.,Li, H.,Baker, L.,Boyle, J.,Blair, L.P.,Chait, B.T.,Patel, D.J.,Aitchison, J.D.,Tackett, A.J.,Allis, C.D. (deposition date: 2006-11-15, release date: 2007-07-03, Last modification date: 2024-10-16) |
| Primary citation | Taverna, S.D.,Ilin, S.,Rogers, R.S.,Tanny, J.C.,Lavender, H.,Li, H.,Baker, L.,Boyle, J.,Blair, L.P.,Chait, B.T.,Patel, D.J.,Aitchison, J.D.,Tackett, A.J.,Allis, C.D. 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 Mol.Cell, 24:785-796, 2006 Cited by PubMed Abstract: 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. PubMed: 17157260DOI: 10.1016/j.molcel.2006.10.026 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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