The chromatin remodeling Isw1a complex is regulated by SUMOylation
| Autor: | Qingtang Shen, Catherine Dargemont, Laura Matabishi-Bibi, Nissrine Beyrouthy |
|---|---|
| Přispěvatelé: | Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Pathologie cellulaire : aspects moléculaires et viraux / Pathologie et Virologie Moléculaire, Institut Universitaire d'Hématologie (IUH), Université Paris Diderot - Paris 7 (UPD7)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins [SDV]Life Sciences [q-bio] SUMO protein Saccharomyces cerevisiae Biology Biochemistry Chromatin remodeling 03 medical and health sciences Nucleosome [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Chromatin structure remodeling (RSC) complex Molecular Biology ChIA-PET ComputingMilieux_MISCELLANEOUS Genetics Adenosine Triphosphatases Isw1a complex Sumoylation [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology Chromatin Assembly and Disassembly Mi-2/NuRD complex Chromatin Cell biology DNA-Binding Proteins 030104 developmental biology biology.protein Protein Binding |
| Zdroj: | Biochemical Journal Biochemical Journal, Portland Press, 2017, 474 (20), pp.3455-3469. ⟨10.1042/BCJ20170172⟩ |
| ISSN: | 0264-6021 1470-8728 |
| DOI: | 10.1042/BCJ20170172⟩ |
| Popis: | The ISWI class of proteins consists of a family of chromatin remodeling ATPases that is ubiquitous in eukaryotes and predominantly functions to slide nucleosomes laterally. The yeast Saccharomyces cerevisiae Isw1 partners with several non-essential alternative subunits — Ioc2, Ioc3, or Ioc4 — to form two distinct complexes Isw1a and Isw1b. Besides its ATPase domain, Isw1 presents a C-terminal region formed by HAND, SANT, and SLIDE domains responsible for interaction with the Ioc proteins and optimal association of Isw1 to chromatin. Despite diverse studies on the functions of the Isw1-containing complexes, molecular evidence for a regulation of this chromatin remodeling ATPase is still elusive. Results presented here indicate that Isw1 is not only ubiquitylated but also strongly SUMOylated on multiple lysine residues by the redundant Siz1/Siz2 SUMO E3 ligases. However, Isw1 is a poor substrate of the Ulp1 and Ulp2 SUMO proteases, thus resulting in a high level of modification. Extensive site-directed mutagenesis allowed us to identify the major SUMOylation sites and develop a SUMO-defective mutant of Isw1. Using this molecular tool, we show that SUMOylation of Isw1 specifically facilitates and/or stabilizes its interaction with its cofactor Ioc3 and consequently the efficient recruitment of the Isw1–Ioc3 complex onto chromatin. Together these data reveal a new regulatory mechanism for this fascinating remodeling factor. |
| Databáze: | OpenAIRE |
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