Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex
Wenping Shi, Lixia Zhao, Yiru Wang, Yi Zhang, Simiao Liu, Yannan Wang, Roger D Kornberg, Heqiao Zhang · 2025
Read Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex by Wenping Shi, Lixia Zhao, Yiru Wang, Yi Zhang, Simiao Liu, Yannan Wang, Roger D Kornberg, Heqiao Zhang (2025) 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-12789522.txt.
Description
Wenping Shi and co-authors capture the structure of a yeast enzyme complex that tags histones in a 2025 paper. The NuA3 complex adds an acetyl tag to one specific lysine on histone H3, shaping gene activity, but how it recognizes its target was unknown. Using cryo-electron microscopy, the team imaged the six-part complex alone, with its fuel molecule, and holding the histone tail.
The pictures show the target lysine sits in a cleft built jointly by the catalytic subunit and a partner subunit. A greasy pocket grips the tail stretch just before the target, while polar contacts along the backbone, especially around one glycine, enforce the exact register. The mechanism explains the complex's strict specificity. The authors frame it as a blueprint for understanding related tagging enzymes.
Catalog record
| CREATOR | Wenping Shi, Lixia Zhao, Yiru Wang, Yi Zhang, Simiao Liu, Yannan Wang, Roger D Kornberg, Heqiao Zhang |
|---|---|
| YEAR | 2025 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 37 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |