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. 2020 Dec 29;22(2):e50967. doi: 10.15252/embr.202050967

Figure 4. HAT1‐mediated non‐histone succinylation specifically targets glycolysis.

Figure 4

  • A
    Diagram showing 7 of 10 key glycolytic enzymes that were identified as HAT1 succinylation targets (red boxes) in the succinylation quantitative proteomics.
  • B
    Bar graphs depicting the relative ratio of succinylation in HAT1 KO versus WT of the 7 key enzymes in the glycolysis pathway depicted in (A). N = 3 biological replicates. Data are presented as mean ± SD.
  • C
    The diagram showed the MS/MS spectra of PGAM1 K99succ peptide for its identification and quantification. The b and y represented the fragment ions of the N and C termini in peptide backbone, respectively. m/z, mass‐to‐charge ratio.
  • D
    The decrease of glucose and increase of lactate in culture medium was measured by ELISA assays in HepG2 cells, HAT1 KO HepG2 cells, and HAT1 KO HepG2 cells reconstituted with either wild‐type HAT1 or mutant HAT1 (T188A). N = 3 biological replicates. Data are presented as mean ± SD. Student's t‐test, **P < 0.01.
  • E, F
    The relative amounts of indicated metabolites were quantified by ELISA assays in HepG2 cells, HAT1 KO HepG2 cells, and HAT1 KO HepG2 cells reconstituted with either wild‐type HAT1 or mutant HAT1 (T188A). N = 3 biological replicates. Data are presented as mean ± SD. Student's t‐test, **P < 0.01; ns, no significance.