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StSIRT1 regulates potato dormancy through deacetylation of peroxidase-like 3 at K37.
Science Advances · · Journal Article
Hu, Dong + more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
StSIRT1-mediated deacetylation of StPRX3 at lysine-37 (K37) suppresses peroxidase activity and is linked to potato dormancy release.
- Why it matters: Dormancy is crucial for plant survival and agronomic performance, yet how posttranslational modification of nonhistone proteins regulates dormancy remains unclear.
- What they did: In potato (Solanum tuberosum L.), StSIRT1 deacetylates StPRX3, lowering K37 acetylation and reducing StPRX3-driven H2O2 scavenging capacity during dormancy release.
- The result: The StPRX3 K37R mutant suppresses peroxidase activity and accelerates dormancy release, revealing an StSIRT1–StPRX3 cascade that reduces H2O2 levels.
The findingWhy it mattersWhat they didThe result