Internet Archive Scholar

PBRM1 BD2 and BD4 associate with RNA to facilitate chromatin association [article]

Saumya M De Silva, Surbhi Sood, Alisha Dhiman, Kilsia F Mercedes, Morkos A Henen, Beat Vogeli, Emily Dykhuizen, Catherine A Musselman
2022 bioRxiv   pre-print

Preserved Fulltext

fulltext thumbnail
Web Archive Capture PDF (2.0 MB)
https://web.archive.org/web/20220210085932/https://www.biorxiv.org/content/biorxiv/early/2022/02/08/2022.02.07.479474.full.pdf

A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2022; you can also visit the original URL. The file type is application/pdf.

PBRM1 is a subunit of the PBAF chromatin remodeling complex, which is mutated in 40-50% of clear cell renal cell carcinoma patients. It is thought to largely function as a chromatin binding subunit of the PBAF complex, but the molecular mechanism underlying this activity is not fully known. PBRM1 contains six tandem bromodomains which are known to cooperate in binding of nucleosomes acetylated at histone H3 lysine 14 (H3K14ac). Here we demonstrate that the second and fourth bromodomains from
more » ... M1 also bind nucleic acids, selectively associating with double stranded RNA elements. Disruption of the RNA binding pocket is found to compromise PBRM1 chromatin binding and inhibit PBRM1-mediated cellular growth effects.
doi:10.1101/2022.02.07.479474 fatcat:xgm2boydvvbl7bytpd7nxnowxa
Citation

Saumya M De Silva, Surbhi Sood, Alisha Dhiman, Kilsia F Mercedes, Morkos A Henen, Beat Vogeli, Emily Dykhuizen, Catherine A Musselman. "PBRM1 BD2 and BD4 associate with RNA to facilitate chromatin association." bioRxiv (2022)