|
|||||
|
|
The histone methyltransferase SUV420H2 and Heterochromatin Proteins HP1 interact but show different dynamic behaviours |
|
| Authors: | Patricia P Souza Pamela Völkel Dave Trinel Julien Vandamme Claire Rosnoblet Laurent Héliot Pierre-Olivier Angrand |
| Institution: | 1. Chromatinomics, Interdisciplinary Research Institute, Université des Sciences et Technologies de Lille/CNRS USR 3078, Parc Scientifique de la Haute Borne, 50 Avenue Halley, F-59658, Villeneuve d'Ascq, France 3. Pathology Department, New York University Langone Medical Center, 550, First Avenue, New York, NY, 10016, USA 2. Biophotonique Cellulaire Fonctionnelle, Interdisciplinary Research Institute, Université des Sciences et Technologies de Lille/CNRS USR 3078, Parc Scientifique de la Haute Borne, 50 Avenue Halley, F-59658, Villeneuve d'Ascq, France 4. Biotech Research & Innovation Centre, University of Copenhagen, Ole Maal?es Vej 5, Copenhagen, DK, 2200, Denmark |
| Abstract: | BackgroundHistone lysine methylation plays a fundamental role in chromatin organization and marks distinct chromatin regions. In particular, trimethylation at lysine 9 of histone H3 (H3K9) and at lysine 20 of histone H4 (H4K20) governed by the histone methyltransferases SUV39H1/2 and SUV420H1/2 respectively, have emerged as a hallmark of pericentric heterochromatin. Controlled chromatin organization is crucial for gene expression regulation and genome stability. Therefore, it is essential to analyze mechanisms responsible for high order chromatin packing and in particular the interplay between enzymes involved in histone modifications, such as histone methyltransferases and proteins that recognize these epigenetic marks. |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ | |