Fig. 1: Lipoylations of key energy metabolism proteins from multiple organisms catalyzed by E. coli-derived LplA in vitro. | Nature Communications

Fig. 1: Lipoylations of key energy metabolism proteins from multiple organisms catalyzed by E. coli-derived LplA in vitro.

From: Boosting energy metabolism and biosynthesis in diverse organisms by a common bacterial salvage lipoylation protein

Fig. 1

a The de novo synthetic pathways and salvage pathway of lipoylation in E. coli, algae, yeast and mammals. b E2 subunits of PDH and OGDH are lipoylated to catalyze the decarboxylation of pyruvate and alpha-ketoglutarate (AKG). c Immunoblots assaying lipoylation of purified, recombinant DLAT and DLST proteins derived from CHO cells in vitro. Data were representative of at least three independent experiments. d Immunoblots assaying lipoylation of purified, recombinant E2 subunits of PDH, OGDH, and GCSH proteins derived from algae in vitro. Data were representative of at least three independent experiments. e Immunoblots assaying lipoylation of purified, recombinant E2 subunits of PDH protein derived from higher plants in vitro. Data were representative of at least three independent experiments. f Immunoblots assaying lipoylation of purified, recombinant Lat1 and Kgd2 proteins derived from yeast S. cerevisiae in vitro. Data were representative of at least three independent experiments. g Sequence logos generated via WebLogo for the conserved lipoyl domain in 17 PDH-E2 and 14 OGDH-E2 proteins from animal, yeast, higher plant, green algae, and cyanobacteria, bacteria (Supplementary Data 2). The conserved lipoylated lysine “K” is marked by a red arrow. h Sequence logos generated via WebLogo for the conserved lipoyl domain in 15 GCSH proteins from animal, yeast, higher plant, green algae, and cyanobacteria, bacteria (Supplementary Data 2). The conserved lipoylated lysine “K” is marked by a red arrow. Immunoblots assaying lipoylation in vitro were performed using lipoic acid and His-tag antibodies as primary antibodies (c–f). ACP acyl-carrier-protein, LDP lipoylation-dependent proteins, LipB/Lip2/LIPT2 octanoyl transferase, LipA/Lip1/LIAS lipoate synthase, Lip3/LIPT1 lipoyl transferase, LplA lipoate protein ligase A, PDH pyruvate dehydrogenase, AKG alpha-ketoglutarate, OGDH alpha-ketoglutarate dehydrogenase, DLAT/Lat1 dihydrolipoamide acetyltransferase, DLST/Kgd2 dihydrolipoamide succinyltransferase. Source data are provided as a Source Data file.

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