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| J. Biol. Chem. Nov (2006); 281(46):35404-12 | |
| Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation- | |
| Dehe PM, Dichtl B, Schaft D, Roguev A, Pamblanco M, Lebrun R, Rodriguez-Gil A, Mkandawire M, Landsberg K, Shevchenko A, Shevchenko A, Rosaleny LE, Tordera V, Chavez S, Stewart AF, Geli V | |
| Laboratoire d'InstabiliteduGenome et Cancerogenese, Institut de Biologie Structurale et Microbiologie, CNRS, Marseille 13402, France- | |
| Abstract: Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex -Set1C- that methylates histone 3 lysine 4 -H3K4-- Here we have determined protein-protein interactions within the complex and related the substructure to function- The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes- The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer- Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc1 strongly interacts with itself- Inactivation of either Bre2 or Sdc1 has very similar effects- Neither is required for complex integrity, and their removal results in an increase of H3K4 mono- and dimethylation and a severe decrease of trimethylation at the 5' end of active coding regions but a decrease of H3K4 dimethylation at the 3' end of coding regions- Cells lacking Spp1 have a reduced amount of Set1 and retain a fraction of trimethylated H3K4, whereas cells lacking Shg1 show slightly elevated levels of both di- and trimethylation- Set1C associates with both serine 5- and serine 2-phosphorylated forms of polymerase II, indicating that the association persists to the 3' end of transcribed genes- Taken together, our results suggest that Set1C subunits stimulate Set1 catalytic activity all along active genes- | |
| [PUBMED: 16921172] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |