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FUS reads histone H3K36me3 to regulate alternative polyadenylation

Nucleic Acids Research. 2024-03; 
Junqi Jia,?Haonan Fan,?Xinyi Wan,?Yuan Fang,?Zhuoning Li,?Yin Tang,?Yanjun Zhang,?Jun Huang,?Dong Fang
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Proteins, Expression, Isolation and Analysis After being rotated at 4°C for 30 min and spun at 13 000 rpm at 4°C for 30 min, the collected supernatants were used to bind with Anti-DYKDDDDK G1 Affinity Resin beads (GenScript, Cat. #L00432) at 4°C overnight. Get A Quote

摘要

Complex organisms generate differential gene expression through the same set of DNA sequences in distinct cells. The communication between chromatin and RNA regulates cellular behavior in tissues. However, little is known about how chromatin, especially histone modifications, regulates RNA polyadenylation. In this study, we found that FUS was recruited to chromatin by H3K36me3 at gene bodies. The H3K36me3 recognition of FUS was mediated by the proline residues in the ZNF domain. After these proline residues were mutated or H3K36me3 was abolished, FUS dissociated from chromatin and bound more to RNA, resulting in an increase in polyadenylation sites far from stop codons genome-wide. A proline mutation correspond... More

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