Structural insights into assembly and function of the RSC chromatin remodeling complex
Autor: | Roberto Dominguez, T. Arakawa, Peter J. Carman, J.M. Reimer, Andres E. Leschziner, Richard W. Baker |
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Rok vydání: | 2020 |
Předmět: |
Saccharomyces cerevisiae Proteins
Protein family Chromosomal Proteins Non-Histone Saccharomyces cerevisiae Cell Cycle Proteins macromolecular substances Article Chromatin remodeling chemistry.chemical_compound 03 medical and health sciences 0302 clinical medicine Structural Biology Translocase Nucleosome RSC complex Amino Acid Sequence Chromatin structure remodeling (RSC) complex Molecular Biology Peptide sequence 030304 developmental biology 0303 health sciences biology Chemistry Cryoelectron Microscopy Nuclear Proteins Chromatin Assembly and Disassembly biology.organism_classification Chromatin Nucleosomes Cell biology DNA-Binding Proteins biology.protein Carrier Proteins DNA Function (biology) 030217 neurology & neurosurgery Transcription Factors |
Zdroj: | Nature structural & molecular biology |
ISSN: | 1545-9985 1545-9993 |
Popis: | Chromatin remodelers regulate the position and composition of nucleosomes throughout the genome, producing different remodeling outcomes despite a shared underlying mechanism based on a conserved RecA DNA translocase. How this functional diversity is achieved remains unknown despite recent cryo-electron microscopy (cryo-EM) reconstructions of several remodelers, including the yeast RSC complex. To address this, we have focused on a RSC subcomplex comprising its ATPase (Sth1), the essential actin-related proteins (ARPs) Arp7 and Arp9, and the fungal-specific protein Rtt102. Combining cryo-EM and biochemistry of this subcomplex, which exhibits regulation of remodeling by the ARPs, we show that ARP binding induces a helical conformation in the HSA domain of Sth1, which bridges the ATPase domain with the bulk of the complex. Surprisingly, the ARP module is rotated by 120° in the subcomplex relative to full RSC about a pivot point previously identified as a regulatory hub in Sth1, suggesting that large conformational changes are part of Sth1 regulation and RSC assembly. We also show that an interaction between Sth1 and the nucleosome acidic patch, which appears to be conserved among SWI/SNF remodelers, enhances remodeling. Taken together, our structural data shed light on the assembly and function of the RSC complex. |
Databáze: | OpenAIRE |
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