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8AV6

CryoEM structure of INO80 core nucleosome complex in closed grappler conformation

Summary for 8AV6
Entry DOI10.2210/pdb8av6/pdb
EMDB information4278
DescriptorRuvB-like helicase, Histone H4, Histone H2A, ... (14 entities in total)
Functional Keywordschromatin remodeler, ino80, actin-related protein, dna binding protein
Biological sourceThermochaetoides thermophila
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Total number of polymer chains20
Total formula weight937641.24
Authors
Kunert, F.,Metzner, F.J.,Eustermann, S.,Jung, J.,Woike, S.,Schall, K.,Kostrewa, D.,Hopfner, K.P. (deposition date: 2022-08-26, release date: 2022-12-14, Last modification date: 2024-07-24)
Primary citationKunert, F.,Metzner, F.J.,Jung, J.,Hopfler, M.,Woike, S.,Schall, K.,Kostrewa, D.,Moldt, M.,Chen, J.X.,Bantele, S.,Pfander, B.,Eustermann, S.,Hopfner, K.P.
Structural mechanism of extranucleosomal DNA readout by the INO80 complex.
Sci Adv, 8:eadd3189-eadd3189, 2022
Cited by
PubMed Abstract: The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by extranucleosomal DNA features. Here, we use cryo-electron microscopy and functional assays to reveal how INO80 binds and is regulated by extranucleosomal DNA. Structures of the regulatory A-module bound to DNA clarify the mechanism of linker DNA binding. The A-module is connected to the motor unit via an HSA/post-HSA lever element to chemomechanically couple the motor and linker DNA sensing. Two notable sites of curved DNA recognition by coordinated action of the four actin/actin-related proteins and the motor suggest how sliding by INO80 can be regulated by extranucleosomal DNA features. Last, the structures clarify the recruitment of YY1/Ies4 subunits and reveal deep architectural similarities between the regulatory modules of INO80 and SWI/SNF complexes.
PubMed: 36490333
DOI: 10.1126/sciadv.add3189
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.68 Å)
Structure validation

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