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Updated: Sep 9, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Pyruvylation expands the redox repertoire of lysine acylation
Jun Seo Park1, Sung Joong Lee2
1Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of Korea; Department of Environmental Materials Science, College of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea.
Abstract:
Song et al. establish lysine pyruvylation (Kpy) as an acylation response to glycolytic flux and pyruvate availability, detect pyruvyl-CoA, implicate histone acetyltransferase 1 and p300 as writers and sirtuin 3 as an eraser, and link promoter-associated histone Kpy to transcriptional regulation, defining a distinct C3 acylation alongside lactylation at the redox-coupled pyruvate-lactate node.
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