6hts: Difference between revisions

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hts OCA], [https://pdbe.org/6hts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hts RCSB], [https://www.ebi.ac.uk/pdbsum/6hts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hts ProSAT]</span></td></tr>

Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. These complexes can be simple, involving one or a few protein subunits, or more complicated multi-subunit machines (1) . Biochemical studies(2-4) have placed the motor domains of several chromatin remodellers in the superhelical location 2 region of the nucleosome. Structural studies of yeast Chd1 and Snf2-a subunit in the complex with the capacity to remodel the structure of chromatin (RSC)-in complex with nucleosomes(5-7) have provided insights into the basic mechanism of nucleosome sliding performed by these complexes. However, how larger, multi-subunit remodelling complexes such as INO80 interact with nucleosomes and how remodellers carry out functions such as nucleosome sliding (8) , histone exchange (9) and nucleosome spacing(10-12) remain poorly understood. Although some remodellers work as monomers (13) , others work as highly cooperative dimers(11, 14, 15). Here we present the structure of the human INO80 chromatin remodeller with a bound nucleosome, which reveals that INO80 interacts with nucleosomes in a previously undescribed manner: the motor domains are located on the DNA at the entry point to the nucleosome, rather than at superhelical location 2. The ARP5-IES6 module of INO80 makes additional contacts on the opposite side of the nucleosome. This arrangement enables the histone H3 tails of the nucleosome to have a role in the regulation of the activities of the INO80 motor domain-unlike in other characterized remodellers, for which H4 tails have been shown to regulate the motor domains.

Structure and regulation of the human INO80-nucleosome complex.,Ayala R, Willhoft O, Aramayo RJ, Wilkinson M, McCormack EA, Ocloo L, Wigley DB, Zhang X Nature. 2018 Apr;556(7701):391-395. doi: 10.1038/s41586-018-0021-6. Epub 2018 Apr, 11. PMID:29643506<ref>PMID:29643506</ref>

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*[[Actin-related protein 3D structures|Actin-related protein 3D structures]]

*[[Histone 3D structures|Histone 3D structures]]

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Aramayo RJ]]

[[Category: Ayala R]]

[[Category: McCormack EA]]

[[Category: Ocloo L]]

[[Category: Wigley DB]]

[[Category: Zhang X]]