Structural mechanism of extranucleosomal DNA readout by the INO80 complex
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Structural mechanism of extranucleosomal DNA readout by the INO80 complex. / Kunert, Franziska; Metzner, Felix J.; Jung, James; Hopfler, Markus; Woike, Stephan; Schall, Kevin; Kostrewa, Dirk; Moldt, Manuela; Chen, Jia Xuan; Bantele, Susanne; Pfander, Boris; Eustermann, Sebastian; Hopfner, Karl Peter.
In: Science Advances, Vol. 8, No. 49, add3189, 2022.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Structural mechanism of extranucleosomal DNA readout by the INO80 complex
AU - Kunert, Franziska
AU - Metzner, Felix J.
AU - Jung, James
AU - Hopfler, Markus
AU - Woike, Stephan
AU - Schall, Kevin
AU - Kostrewa, Dirk
AU - Moldt, Manuela
AU - Chen, Jia Xuan
AU - Bantele, Susanne
AU - Pfander, Boris
AU - Eustermann, Sebastian
AU - Hopfner, Karl Peter
N1 - Publisher Copyright: © 2022 The Authors.
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
U2 - 10.1126/sciadv.add3189
DO - 10.1126/sciadv.add3189
M3 - Journal article
C2 - 36490333
AN - SCOPUS:85143917546
VL - 8
JO - Science advances
JF - Science advances
SN - 2375-2548
IS - 49
M1 - add3189
ER -
ID: 336465026