Asset Details
Do you wish to reserve the book?
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA
Do you wish to request the book?
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA
2017
Overview
Biochemical reconstitution of PRC2 interactions with chromatinized templates demonstrates that protein-free linker DNA dominates the PRC2-nucleosome interaction, while RNA inhibits binding.
Many studies have revealed pathways of epigenetic gene silencing by Polycomb repressive complex 2 (PRC2)
in vivo
, but understanding the underlying molecular mechanisms requires biochemistry. Here we analyze interactions of reconstituted human PRC2 with nucleosome complexes. Histone modifications, the H3K27M cancer mutation, and inclusion of JARID2 or EZH1 in the PRC2 complex have unexpectedly minor effects on PRC2–nucleosome binding. Instead, protein-free linker DNA dominates the PRC2–nucleosome interaction. Specificity for CG-rich sequences is consistent with PRC2 occupying CG-rich DNA
in vivo
. PRC2 preferentially binds methylated DNA regulated by its AEBP2 subunit, suggesting how DNA and histone methylation collaborate to repress chromatin. We find that RNA, known to inhibit PRC2 activity, is not a methyltransferase inhibitor
per se
. Instead, RNA sequesters PRC2 from nucleosome substrates, because PRC2 binding requires linker DNA, and RNA and DNA binding are mutually exclusive. Together, we provide a model for PRC2 recruitment and an explanation for how actively transcribed genomic regions bind PRC2 but escape silencing.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ 38/71
/ 42/34
/ 45/70
/ 45/77
/ 82/16
/ 82/80
/ 82/83
/ Binding
/ Cancer
/ DNA
/ DNA-Binding Proteins - genetics
/ Epigenesis, Genetic - genetics
/ Humans
/ Mutation
/ Polycomb Repressive Complex 2 - genetics
/ Proteins
/ Repressor Proteins - metabolism
/ RNA
