Nucleosomal regulation of chromatin composition and nuclear assembly revealed by histone depletion

Autor: Zierhut, C., Jenness, C., Kimura, Hiroshi, Funabiki, H.
Rok vydání: 2014
Předmět:
Proteomics
Histones/*metabolism
Nuclear Envelope
DNA-Binding Proteins/genetics/metabolism/physiology
Nuclear Proteins/genetics/metabolism/physiology
Cell Cycle Proteins
Spindle Apparatus
Solenoid (DNA)
Xenopus Proteins
Biology
Article
Chromatin remodeling
Histones
Xenopus laevis
Histone H1
Structural Biology
Histone methylation
Guanine Nucleotide Exchange Factors
Animals
DNA/metabolism
Nucleosome
Histone code
Guanine Nucleotide Exchange Factors/genetics/metabolism/physiology
Molecular Biology
Nuclear Envelope/metabolism
Nucleosomes/*metabolism/physiology
Spindle Apparatus/metabolism
Transcription Factors/genetics/metabolism/physiology
Models
Genetic
Xenopus Proteins/genetics/metabolism/physiology
Cell Cycle Proteins/genetics/metabolism/physiology
Nuclear Proteins
DNA
Nuclear Pore/metabolism
Chromatin Assembly and Disassembly
Molecular biology
Linker DNA
Nucleosomes
Cell biology
DNA-Binding Proteins
Histone
Nuclear Pore
biology.protein
Transcription Factors
Zdroj: Nature Structural & Molecular Biology. 21:617-625
ISSN: 1545-9985
1545-9993
DOI: 10.1038/nsmb.2845
Popis: A new system to monitor the effects of nucleosome depletion in Xenopus egg extracts reveals that nucleosomes are required for spindle assembly and for recruitment of nuclear pore complex (NPC) components to the nuclear envelope for NPC formation. Nucleosomes are the fundamental unit of chromatin, but analysis of transcription-independent nucleosome functions has been complicated by the gene-expression changes resulting from histone manipulation. Here we solve this dilemma by developing Xenopus laevis egg extracts deficient for nucleosome formation and by analyzing the proteomic landscape and behavior of nucleosomal chromatin and nucleosome-free DNA. We show that although nucleosome-free DNA can recruit nuclear-envelope membranes, nucleosomes are required for spindle assembly and for formation of the lamina and of nuclear pore complexes (NPCs). We show that, in addition to the Ran G-nucleotide exchange factor RCC1, ELYS, the initiator of NPC formation, fails to associate with naked DNA but directly binds histone H2A–H2B dimers and nucleosomes. Tethering ELYS and RCC1 to DNA bypasses the requirement for nucleosomes in NPC formation in a synergistic manner. Thus, the minimal essential function of nucleosomes in NPC formation is to recruit RCC1 and ELYS.
Databáze: OpenAIRE
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