Fig. 7: Auto-lactylation of HAT1 on K15 promotes the lactylation of RPA1.

A Detection of HA-Trap binded acetyltransferase in cells overexpressed 8 acetyltransferase of KAT family, including P300, CBP, HAT1, KAT2A, KAT2B, KAT5, KAT7 and KAT8. B The level of lactylated acetyltransferases in cells overexpressed 8 acetyltransferase of KAT family, including P300, CBP, HAT1, KAT2A, KAT2B, KAT5, KAT7, and KAT8 (the red arrows represent the corresponding lactylated proteins). C The expression of acetyltransferase in whole cell lysates overexpressed 8 acetyltransferase of KAT family, including P300, CBP, HAT1, KAT2A, KAT2B, KAT5, KAT7, and KAT8. D Secondary mass spectrometry map of HAT5 K15 lactylation modification. E Sequence alignment of the K15 site of HAT1 in diverse species. F The level of NALA-induced lactylated HAT1 in 293 T cells. G The expression of lactylated HAT1 in WT cells as well as in mutant cells with HAT1 K15R. H The level of lactylated RPA1 in HAT1-WT cells as well as in mutant cells with HAT1-K15R. I Relative HR efficiency in WT cells and in mutant cells with HAT1-K15R. J The IR-induced foci of RPA1 in A549 cells expressing HAT1-WT proteins or mutant HAT1-K15R (scale bar=5 μm; n = 25). K The colony-forming ability of A549 cells expressing HAT1-WT proteins or mutant HAT1-K15R. All data were analyzed using two-way analysis of variance (ANOVA), **P < 0.01.