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Cryo-EM 3D maps of the S. cerevisiae Yta7 bound to ATPgS and histone H3 tail


ABSTRACT:

SUBMITTER: Feng Wang 

PROVIDER: EMPIAR-11852 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

The Saccharomyces cerevisiae Yta7 ATPase hexamer contains a unique bromodomain tier that functions in nucleosome disassembly.

Wang Feng F   Feng Xiang X   He Qing Q   Li Hua H   Li Huilin H  

The Journal of biological chemistry 20221230 2


The Saccharomyces cerevisiae Yta7 is a chromatin remodeler harboring a histone-interacting bromodomain (BRD) and two AAA+ modules. It is not well understood how Yta7 recognizes the histone H3 tail to promote nucleosome disassembly for DNA replication or RNA transcription. By cryo-EM analysis, here we show that Yta7 assembles a three-tiered hexamer with a top BRD tier, a middle AAA1 tier, and a bottom AAA2 tier. Unexpectedly, the Yta7 BRD stabilizes a four-stranded β-helix, termed BRD-interacting  ...[more]

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