The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling
| Autor: | Alessandro Tosi, Philipp Korber, Marianne Schwarz, Gabriele Stoehr, Karl-Peter Hopfner, Sebastian Eustermann, Kevin Schall, Vanessa Niebauer, Kilian R. Knoll, Elisa Oberbeckmann, Andrea Buchfellner |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Protein Conformation Saccharomyces cerevisiae Chromatin remodeling 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Protein structure Structural Biology Nucleosome Amino Acid Sequence DNA Fungal Molecular Biology Actin Cell Nucleus biology Sequence Homology Amino Acid Microfilament Proteins biology.organism_classification Chromatin Assembly and Disassembly Linker DNA Cell biology Chromatin 030104 developmental biology chemistry 030217 neurology & neurosurgery DNA |
| Zdroj: | Nature structuralmolecular biology. 25(9) |
| ISSN: | 1545-9985 |
| Popis: | Nuclear actin (N-actin) and actin-related proteins (Arps) are critical components of several chromatin modulating complexes, including the chromatin remodeler INO80, but their function is largely elusive. Here, we report the crystal structure of the 180-kDa Arp8 module of Saccharomyces cerevisiae INO80 and establish its role in recognition of extranucleosomal linker DNA. Arp8 engages N-actin in a manner distinct from that of other actin-fold proteins and thereby specifies recruitment of the Arp4–N-actin heterodimer to a segmented scaffold of the helicase-SANT-associated (HSA) domain of Ino80. The helical HSA domain spans over 120 A and provides an extended binding platform for extranucleosomal entry DNA that is required for nucleosome sliding and genome-wide nucleosome positioning. Together with the recent cryo-electron microscopy structure of INO80Core–nucleosome complex, our findings suggest an allosteric mechanism by which INO80 senses 40-bp linker DNA to conduct highly processive chromatin remodeling. X-ray crystal structures and mutational analysis of the Arp8 module of the yeast chromatin remodeler INO80 reveal its function as a linker DNA sensor required for nucleosome positioning. |
| Databáze: | OpenAIRE |
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