Regulation of DNA Translocation Efficiency within the Chromatin Remodeler RSC/Sth1 Potentiates Nucleosome Sliding and Ejection
Autor: | Yongli Zhang, Bradley R. Cairns, Heather Szerlong, George Sirinakis, Margaret M. Kasten, Timothy J. Parnell, Cedric R. Clapier, Ramya Viswanathan |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Time Factors animal structures Cell Cycle Proteins Saccharomyces cerevisiae DNA-binding protein Article 03 medical and health sciences chemistry.chemical_compound Adenosine Triphosphate ATP hydrolysis Nucleosome Protein Interaction Domains and Motifs Chromatin structure remodeling (RSC) complex DNA Fungal Molecular Biology Transcription factor Binding Sites biology Hydrolysis Microfilament Proteins Fungal genetics Nuclear Proteins Biological Transport Cell Biology Chromatin Assembly and Disassembly Molecular biology Nucleosomes Chromatin Cell biology DNA-Binding Proteins 030104 developmental biology chemistry Mutation biology.protein DNA Protein Binding Transcription Factors |
Zdroj: | Molecular Cell. 62:453-461 |
ISSN: | 1097-2765 |
Popis: | The RSC chromatin remodeler slides and ejects nucleosomes, utilizing a catalytic subunit (Sth1) with DNA translocation activity, which can pump DNA around the nucleosome. A central question is whether and how DNA translocation is regulated to achieve sliding versus ejection. Here, we report the regulation of DNA translocation efficiency by two domains residing on Sth1 (Post-HSA and Protrusion 1), and by actin-related proteins (ARPs) which bind Sth1. ARPs facilitated sliding and ejection by improving ‘coupling’ – the amount of DNA translocation by Sth1 relative to ATP hydrolysis. We also identified and characterized Protrusion 1 mutations that promote ‘coupling’, and Post-HSA mutations that improve ATP hydrolysis; notably, the strongest mutations conferred efficient nucleosome ejection without ARPs. Taken together, sliding-to-ejection involves a continuum of DNA translocation efficiency, consistent with higher magnitudes of ATPase and coupling activities (involving ARPs and Sth1 domains), enabling the simultaneous rupture of multiple histone-DNA contacts facilitating ejection. |
Databáze: | OpenAIRE |
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