دورية أكاديمية
Mechanistic Insights into Autoinhibition of the Oncogenic Chromatin Remodeler ALC1.
| العنوان: | Mechanistic Insights into Autoinhibition of the Oncogenic Chromatin Remodeler ALC1. |
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| المؤلفون: | Lehmann LC; Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124 Uppsala, Sweden., Hewitt G; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK., Aibara S; Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165 Solna, Sweden., Leitner A; Department of Biology, Institute of Molecular Systems Biology, Swiss Federal Institute of Technology, 8093 Zürich, Switzerland., Marklund E; Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124 Uppsala, Sweden., Maslen SL; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK., Maturi V; Department of Medical Biochemistry and Microbiology, and Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, 75123 Uppsala, Sweden., Chen Y; Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124 Uppsala, Sweden., van der Spoel D; Department of Cell and Molecular Biology, Computational Biology and Bioinformatics, Uppsala University, 75124 Uppsala, Sweden., Skehel JM; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK., Moustakas A; Department of Medical Biochemistry and Microbiology, and Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, 75123 Uppsala, Sweden., Boulton SJ; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: simon.boulton@crick.ac.uk., Deindl S; Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124 Uppsala, Sweden. Electronic address: sebastian.deindl@icm.uu.se. |
| المصدر: | Molecular cell [Mol Cell] 2017 Dec 07; Vol. 68 (5), pp. 847-859.e7. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print Cited Medium: Internet ISSN: 1097-4164 (Electronic) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Cambridge Ma : Cell Press Original Publication: Cambridge, Mass. : Cell Press, c1997- |
| مواضيع طبية MeSH: | Chromatin Assembly and Disassembly* , DNA Damage* , DNA Repair*, DNA Helicases/*metabolism , DNA-Binding Proteins/*metabolism , Nucleosomes/*enzymology, Catalytic Domain ; Cell Line, Tumor ; DNA Helicases/chemistry ; DNA Helicases/genetics ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; Enzyme Activation ; Humans ; Microscopy, Electron ; Molecular Dynamics Simulation ; Mutation ; Nucleosomes/chemistry ; Poly (ADP-Ribose) Polymerase-1/chemistry ; Poly (ADP-Ribose) Polymerase-1/metabolism ; Poly ADP Ribosylation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Transport ; Scattering, Small Angle ; Static Electricity ; Structure-Activity Relationship ; Time Factors ; X-Ray Diffraction |
| مستخلص: | Human ALC1 is an oncogene-encoded chromatin-remodeling enzyme required for DNA repair that possesses a poly(ADP-ribose) (PAR)-binding macro domain. Its engagement with PARylated PARP1 activates ALC1 at sites of DNA damage, but the underlying mechanism remains unclear. Here, we establish a dual role for the macro domain in autoinhibition of ALC1 ATPase activity and coupling to nucleosome mobilization. In the absence of DNA damage, an inactive conformation of the ATPase is maintained by juxtaposition of the macro domain against predominantly the C-terminal ATPase lobe through conserved electrostatic interactions. Mutations within this interface displace the macro domain, constitutively activate the ALC1 ATPase independent of PARylated PARP1, and alter the dynamics of ALC1 recruitment at DNA damage sites. Upon DNA damage, binding of PARylated PARP1 by the macro domain induces a conformational change that relieves autoinhibitory interactions with the ATPase motor, which selectively activates ALC1 remodeling upon recruitment to sites of DNA damage. (Copyright © 2017 Elsevier Inc. All rights reserved.) |
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| معلومات مُعتمدة: | United Kingdom WT_ Wellcome Trust; 11581 United Kingdom CRUK_ Cancer Research UK; MC_U105178788 United Kingdom MRC_ Medical Research Council |
| فهرسة مساهمة: | Keywords: ADP-ribosylation; ATP-dependent chromatin remodeler; ATPase; DNA repair; PARP; allosteric regulation; allostery; chromatin remodeling; macro domain; structure |
| المشرفين على المادة: | 0 (DNA-Binding Proteins) 0 (Nucleosomes) EC 2.4.2.30 (PARP1 protein, human) EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1) EC 3.6.4.- (DNA Helicases) EC 3.6.4.12 (CHD1L protein, human) |
| تواريخ الأحداث: | Date Created: 20171209 Date Completed: 20171226 Latest Revision: 20240210 |
| رمز التحديث: | 20240210 |
| مُعرف محوري في PubMed: | PMC5745148 |
| DOI: | 10.1016/j.molcel.2017.10.017 |
| PMID: | 29220652 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1097-4164 |
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| DOI: | 10.1016/j.molcel.2017.10.017 |