Objectif Protein methylation at lysine residues modulates chromatin structure, affects gene expression and mammalian development. Recently, it was also shown to influence the stability and activity of non-histone proteins. Lysine methylation marks manifest their biological effect via so-called ‘readers’ (or reading domains) which recognize and bind the methylation mark and directly alter the chromatin structure or act as a scaffold for other proteins, which induce biological responses. Reading domains include Plant homeodomains (PHD) and Chromodomains (CD) found in many chromatin proteins. KMET-READ plans to investigate the biological role of these reading domains in essential histone lysine methyltransferases - PHDs in MLL2 and MLL3 and CDs in SUV39H1 and SUV39H2. The results obtained here will advance the understanding of chromatin changes in human cells. The proposal will apply an interdisciplinary approach in an international environment to maximize its chances of success: the biological role of reading domains will be evaluated with molecular biology (histone and chromatin pulldowns, ChIP-seq, confocal microscopy), biochemistry (Peptide arrays, mass spectrometry, methyltransferase activity assays) and biophysics techniques (fluorescence anisotropy, circular dichroism spectroscopy) as well as crystallography (solving the structure of reading domains). Importantly, the KMET-READ project will also develop a yeast-3-hybrid method for the identification of new reading domains, which will allow to discover binding partners for just recently characterized new protein methylation marks. This novel method will be patented and introduced into market. All project partners will ensure an efficient dissemination and communication of the results of the KMET-READ project. The project will provide excellent training in research methods and other skills for the fellow that will strongly support her future career and initiate new and sustainable collaborations between the partners. Champ scientifique natural sciencesbiological sciencesbiochemistrybiomoleculesproteinsproteomicsnatural sciencesearth and related environmental sciencesgeologymineralogycrystallographynatural sciencesphysical sciencesopticsmicroscopyconfocal microscopynatural scienceschemical sciencesorganic chemistryaminesnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsenzymes Programme(s) H2020-EU.1.3. - EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions Main Programme H2020-EU.1.3.2. - Nurturing excellence by means of cross-border and cross-sector mobility Thème(s) MSCA-IF-2014-EF - Marie Skłodowska-Curie Individual Fellowships (IF-EF) Appel à propositions H2020-MSCA-IF-2014 Voir d’autres projets de cet appel Régime de financement MSCA-IF-EF-ST - Standard EF Coordinateur UNIVERSITY OF STUTTGART Contribution nette de l'UE € 171 460,80 Adresse KEPLERSTRASSE 7 70174 Stuttgart Allemagne Voir sur la carte Région Baden-Württemberg Stuttgart Stuttgart, Stadtkreis Type d’activité Higher or Secondary Education Establishments Liens Contacter l’organisation Opens in new window Site web Opens in new window Participation aux programmes de R&I de l'UE Opens in new window Réseau de collaboration HORIZON Opens in new window Coût total € 171 460,80
