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Structural mechanism of extranucleosomal DNA readout by the INO80 complex.
Kunert, Franziska; Metzner, Felix J; Jung, James; Höpfler, Markus; Woike, Stephan; Schall, Kevin; Kostrewa, Dirk; Moldt, Manuela; Chen, Jia-Xuan; Bantele, Susanne; Pfander, Boris; Eustermann, Sebastian; Hopfner, Karl-Peter.
Afiliación
  • Kunert F; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Metzner FJ; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Jung J; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Höpfler M; DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Martinsried, Germany.
  • Woike S; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Schall K; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Kostrewa D; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Moldt M; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Chen JX; Institute of Molecular Biology (IMB), Mainz, Germany.
  • Bantele S; DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Martinsried, Germany.
  • Pfander B; DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Martinsried, Germany.
  • Eustermann S; Gene Center, Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
  • Hopfner KP; European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Sci Adv ; 8(49): eadd3189, 2022 Dec 09.
Article en En | MEDLINE | ID: mdl-36490333
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Sci Adv Año: 2022 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Sci Adv Año: 2022 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos