In-cell histone acetylation
reaction by PLIED/1. A, Subcellular
localization of PLIED. eDHFR-FLAG- or PLIED-FLAG-transfected HEK293T
cells were treated with nocodazole (330 nM) for 4 h, followed by TMP-TAMRA
(10 μM, chemical structure is shown in Figure S3A) with nocodazole for 1 h. DNA was stained with Hoechst
33342 to visualize chromatin distribution. Representative images of
mitotic cells are shown. Scale bar, 10 μm. B, In-cell histone
acetylation by PLIED/1 systems. eDHFR-FLAG- or PLIED-FLAG-transfected
HEK293T cells were incubated with or without acetyl donor 2 (100 μM) and TMP-BAHA 1 (1 μM) at 37 °C
for 5 h. Whole-cell extracts were immunoblotted with anti-H2BK120ac
antibody. The expressed eDHFR derivatives and histones were visualized
by Oriole staining. Representative data of two independent experiments
are shown. C, Acetylation yields of indicated lysine residues on histones
from PLIED/1-treated HEK293T cells as in B. The yield
was determined by LC–MS/MS. D, Optimization of histone acetylation
by PLIED-L52. PLIED-L52-FLAG-transfected HEK293T cells were incubated
with TMP-BAHA 1 and acetyl donor 2 at the
indicated concentrations at 37 °C for 5 h. E, Time course analysis
of histone acetylation by PLIED-L52/1. PLIED-L52-FLAG-transfected
HEK293T cells were incubated with TMP-BAHA 1 (5 μM)
and acetyl donor 2 (200 μM) at 37 °C for the
indicated time. Acetylation yields were analyzed by LC–MS/MS.
For LC–MS/MS data, error bars represent the range of two independent
experiments (C–E). F, Histone-selectivity of PLIED-L52/1-mediated acetylation. PLIED-L52-FLAG-transfected HEK293T
cells were incubated with or without TMP-BAHA 1 (5 μM)
in the presence of acetyl donor 2 (200 μM) at 37
°C for 5 or 10 h. For knockdown of RNF20, HEK293T cells were
transfected with control or RNF20 siRNA and harvested after 10 h.
The lysine acetylation levels of proteins in the whole-cell extract
were detected by immunoblotting using anti-AcK antibody. Proteins
were visualized by CBB staining. Representative data of two independent
experiments are shown. G, Immunoblotting analysis of the PLIED-L52/1-mediated in-cell acetylation. HEK293T cells were treated
as in F. To assess levels of RNF20, whole-cell extracts were immunoblotted
with anti-RNF20. β-Actin was used as a loading control. To assess
levels of histone PTMs, histones were acid-extracted from the cells
and analyzed by immunoblotting with the indicated antibodies. The
loading amounts of histones were visualized with Oriole staining.
Representative data of two independent experiments are shown.