Figure 3: Mitochondrial acetylation overlaps at a site-specific level between an hst4Δ mutant and a biotin-starved WT. | Nature Communications

Figure 3: Mitochondrial acetylation overlaps at a site-specific level between an hst4Δ mutant and a biotin-starved WT.

From: Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p

Figure 3

(a) The cellular distribution of regulated acetylation sites for sirtuin deacetylases Sir2p, Hst2p and Hst4p. Total number of quantified sites are shown below. (b) GO annotation of regulated proteins compared with their respective genome abundance from the hst4Δ acetylation experiment. (c) Hierarchical cluster analysis of commonly identified lysine acetylation sites in sirtuin mutants and biotin-starved WT. (d) The NAD+ salvage pathway. NAD+ is converted to nicotinamide during high level of sirtuin deacetylase activity at nutrient-low conditions. Through enzymatic activities of Pnc1p and Npt1p, nicotinamide is converted to nicotinic acid mononucleotide (NaMN). (e) The flux through the NAD+ salvage pathway in WT cells with or without biotin compared with pnc1Δ and hst4Δ mutant strains. [14C]-nicotinamide conversion to NaMN measured by scintillation normalized to the amount of protein. Error bars indicate s.d. in three biological replica experiments.

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