Figure 1. Increased lysine acetylation of mitochondrial proteins involved in multiple mitochondrial energy transduction pathways in cardiac tissue of mice from the heart failure group.

(A) Lysine-acetylated proteins (indicated by circles, protein symbols are noted) identified by mass spectrometry in both heart failure (HF) samples and sham-operated control samples (n = 2/group) in each of the 3 main mitochondrial fuel oxidation/ATP synthesis pathways (β-oxidation, tricarboxylic acid [TCA] cycle, and electron transport complex [ETC]). All acetylated residues with at least ± 1.5 fold change for mean HF/control values are shown. Specific lysine acetylation sites are noted in parentheses. Acetylation status is indicated by color coding: proteins with increased acetylation (HF/sham) are in red; proteins with decreased acetylation are in blue; and proteins with no change are in gray. (B) All detected acetylated mitochondrial proteins were rank ordered according to log₂ fold change between compensated hypertrophy (CH) or HF and their corresponding sham controls in mean protein abundance along the x axis (blue circles). The log₂ fold change between CH or HF and corresponding sham controls of each detected acetyl isoform (red squares, normalized to corresponding protein abundance) is plotted on the y axis in the same position on the x axis as the corresponding protein. The dashed line represents no change in acetylation level. Additional numerical data is provided in Supplemental Tables 2-4. SDHA, succinate dehydrogenase A.