An E2 ubiquitin-conjugating enzyme links diubiquitinated H2B to H3K27M oncohistone function
Alan L. Jiao, Erdem Sendinc, Barry M. Zee, Felice Wallner, Yang Shi · 2024
Read An E2 ubiquitin-conjugating enzyme links diubiquitinated H2B to H3K27M oncohistone function by Alan L. Jiao, Erdem Sendinc, Barry M. Zee, Felice Wallner, Yang Shi (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11621828.txt.
Description
Alan Jiao and co-authors hunt for genes that soften a deadly childhood brain tumor mutation, in work from 2024. The H3K27M oncohistone drives most diffuse midline gliomas and wipes out a protective chemical mark on chromatin.
Using worms engineered with the same mutation, the team screened the whole genome for suppressors. Twenty turned up, and nineteen sat in the very histone gene carrying the mutation, changing how it grips its partner complex. The twentieth hit was an enzyme that tags another histone, H2B, with two ubiquitin marks. Deleting it restored the protective mark to nearly half its normal level despite the oncohistone's presence. The finding suggests tweaking that tagging could blunt the tumor's driver.
Catalog record
| CREATOR | Alan L. Jiao, Erdem Sendinc, Barry M. Zee, Felice Wallner, Yang Shi |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 40 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |