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Updated: Aug 30, 2026

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
Published on: January 26, 2024
Expression of histone acetyltransferases was down-regulated in poly(ADP-ribose) polymerase-1-deficient murine cells
Katsuya Ota1, Masanori Kameoka, Yasuharu Tanaka
1Department of Biochemistry, Nara Medical University, Shijo 840, Kashihara, Nara 634-8521, Japan.
Abstract:
NF-kappaB-dependent, as well as human immunodeficiency virus type-1 (HIV-1) long terminal repeat (LTR)-dependent, reporter gene expression was significantly impaired in cells derived from poly(ADP-ribose) polymerase-1 (PARP-1)-knockout (PARP-1 -/-) mice. In addition, the level of protein acetylation was markedly lower in PARP-1 -/- cells than control (PARP-1 +/+) cells. Surprisingly, the expression levels of histone acetyltransferases (HATs), p300, cAMP response element-binding protein-binding protein (CBP), and p300/CBP-associated factor (PCAF), were significantly reduced in PARP-1 -/- cells, as compared with PARP-1 +/+ cells. These results suggest that PARP-1 is required for the proper expression of particular HATs. Since p300 and CBP are coactivators of NF-kappaB, we propose here that PARP-1 participates in NF-kappaB-dependent transcription by means of maintaining the expression of HATs.
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