The intrinsically disordered N-terminal region of eIF5B nucleates RNA-driven phase separation
Recently, we found that eukaryotic Initiation Factor 5B (eIF5B) forms cytoplasmic puncta under conditions of cellular stress and that the puncta formation drives an increase in alternative translation initiation. The formation of these puncta depends on the intrinsically disordered N-terminal region of eIF5B (eIF5B-NTR). To address the driving force behind this observation, we reconstituted a…
TET1, a crucial DNA demethylase for mammalian embryonic development, is shown to be recruited to its chromatin substrate through a novel N-terminal region. This region directly binds nucleosomes and enhances chromatin binding in mouse embryonic stem cells. The presence of this region was confirmed via fluorescence recovery after photobleaching during interphase and retention of chromosomes during mitosis.
A high-resolution cryo-EM structure of the TET1-nucleosome complex reveals that the recognition of the acidic patch on the nucleosome occurs through a canonical arginine anchor located at position R75, with additional contacts along the H2B surface. This interaction, validated through biochemical and cellular analyses, contributes to TET1's chromatin engagement.
Importantly, this region is absent in TET2 and TET3, indicating that direct nucleosome recognition is a unique feature of TET1. The findings uncover a new chromatin-binding module in TET1 and provide a structural basis for its interaction with nucleosomes.
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