Extended Data Fig. 3: TPI1 regulates global histone acetylation via altering DHAP (Related to Fig. 2).
a, TPI1F278L is defective in glycolytic activity. The specific activities of TPI1 and TPI1F278L were analyzed, relative (to TPI1) specific activity of both enzymes were presented. n = 3 biologically independent experiments (P < 0.0001). b, TPI1F278L localized to nucleus and cytoplasm. The cellular compartmentation of TPI1F278L was detected by immunofluorescence. Scale bar: 10um. c, TPI1 overexpression decreased HDACs activities. The HDACs activities were compared between nucleus of HeLa cells and of HeLa cells overexpressing TPI1. n = 3 biologically independent samples (P = 0.0009). d, HDACs revered TPI1 effects on histone acetylation. The pan- and site specific histone acetylation levels were compared among HeLa cells, TPI1-expressing HeLa cells and HeLa cells that co-expressing TPI1 and each of HDAC1, HDAC2 or HDAC3. e, DHAP treatment increased nuclear DHAP levels. 0.5 mM DHAP was supplemented in the DMEM that was used to culture HeLa cells. The nuclear DHAP levels were measured for both untreated and treated cells. n = 3 biologically independent samples (P < 0.0001). f, DHAP decrease global histone acetylation. Histone acetylation levels were detected in HEK293T cells cultured without and with DHAP as indicated concentrations in the culture media. g, GAP treatment increased nuclear GAP levels. 0.5 mM GAP was supplemented in the DMEM that was used to culture HEK293T cells. The nuclear GAP levels were measured for both untreated and treated cells. n = 3 biologically independent samples (P < 0.0001).
