A unique binding mode enables MCM2 to chaperone histones H3–H4 at replication forks

Chromatin reassembly after replication requires recycling of old and deposition of new histones. Structural insights into how MCM2, part of the replicative helicase, interacts with H3–H4 suggest a function in histone recycling at replication forks. During DNA replication, chromatin is reassembled by...

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Veröffentlicht in:	Nature structural & molecular biology 2015-08, Vol.22 (8), p.618-626
Hauptverfasser:	Huang, Hongda, Strømme, Caroline B, Saredi, Giulia, Hödl, Martina, Strandsby, Anne, González-Aguilera, Cristina, Chen, Shoudeng, Groth, Anja, Patel, Dinshaw J
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/535/1266 631/535 631/57 Amino Acid Sequence Biochemistry Biological Microscopy Blotting, Western Cell Line, Tumor Chromatin - chemistry Chromatin - genetics Chromatin - metabolism Deoxyribonucleic acid DNA DNA - chemistry DNA - genetics DNA - metabolism DNA Replication Genomes HeLa Cells Histones - chemistry Histones - genetics Histones - metabolism Humans Life Sciences Membrane Biology Minichromosome Maintenance Complex Component 2 - chemistry Minichromosome Maintenance Complex Component 2 - genetics Minichromosome Maintenance Complex Component 2 - metabolism Models, Molecular Molecular chaperones Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Molecular Sequence Data Mutation Nucleic Acid Conformation Physiological aspects Protein Binding Protein Multimerization Protein Structure Protein Structure, Tertiary RNA Interference Sequence Homology, Amino Acid Structure
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