Fungal enzyme structure offers clues to RNA modification
Experiments with purified fungal protein revealed a heart-shaped pair and suggested that RNA positioning, rather than binding strength, drives its chemical modification.
Our read
Mechanisms- Studied:
- Study of purified fungal proteins
- What changed:
- tRNA acetylation was enabled by two conserved active site residues and two basic patches
- The catch:
- The structural work examined synthetic probes, not an enzyme bound to RNA
- In the record:
- One of 26 papers on NAT10 on record: 12 with results in people, 4 in animals.
- Why it’s aging research:
- Something that builds up with age.
Editor of record: Boris Djordjevic · AgingResearch.News
In experiments with purified protein from the fungus Chaetomium thermophilum, researchers mapped NAT10, an enzyme that adds chemical tags called acetyl groups to RNA. They used cryo-electron microscopy, which images frozen samples, to examine the enzyme bound to specially designed chemical probes. NAT10 formed a symmetrical, heart-shaped pair.
Biochemical experiments identified two sites in the enzyme’s reaction center and two positively charged surface patches that enabled tagging of transfer RNA, which helps cells build proteins. Tests with a helper protein suggested that RNA’s orientation, rather than how tightly it bound, drove the reaction. Separate experiments found that NAT10’s tagging activity was required for yeast growth at high temperatures and for senescence—a state in which cells stop dividing—induced by the drug etoposide in human lung fibroblasts, connective-tissue cells grown in the lab.
Why it matters
Problems with NAT10 regulation have been associated with premature aging syndromes. Understanding its RNA-tagging activity provides a starting point for investigating that connection.
Caveats
The structural work examined purified fungal protein with synthetic probes, not an enzyme bound to RNA. The human-cell findings concerned drug-induced senescence, not natural aging or effects in people.
The paper
Structure of the NAT10 acetyltransferase and mechanism of tRNA acetylation
University of Pennsylvania
Nature Communications, Jun 20, 2026, Open access
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