Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.

Abstract:

:'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming1,2. Pioneer factors can bind nucleosomal DNA to enable gene expression from regions of the genome with closed chromatin. SOX2 is a prominent pioneer factor that is essential for pluripotency and self-renewal of embryonic stem cells3. Here we report cryo-electron microscopy structures of the DNA-binding domains of SOX2 and its close homologue SOX11 bound to nucleosomes. The structures show that SOX factors can bind and locally distort DNA at superhelical location 2. The factors also facilitate detachment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility. SOX-factor binding to the nucleosome can also lead to a repositioning of the N-terminal tail of histone H4 that includes residue lysine 16. We speculate that this repositioning is incompatible with higher-order nucleosome stacking, which involves contacts of the H4 tail with a neighbouring nucleosome. Our results indicate that pioneer transcription factors can use binding energy to initiate chromatin opening, and thereby facilitate nucleosome remodelling and subsequent transcription.

journal_name

Nature

journal_title

Nature

authors

Dodonova SO,Zhu F,Dienemann C,Taipale J,Cramer P

doi

10.1038/s41586-020-2195-y

subject

Has Abstract

pub_date

2020-04-01 00:00:00

pages

669-672

issue

7805

eissn

0028-0836

issn

1476-4687

pii

10.1038/s41586-020-2195-y

journal_volume

580

pub_type

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