A novel multidomain acyl-CoA carboxylase in Saccharopolyspora erythraea provides malonyl-CoA for de novo fatty acid biosynthesis
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Nature
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Acetyl-CoA carboxylases (ACCs) are enzyme complexes generally composed of three catalytic domains
and distributed in all organisms. In prokaryotes and plastids of most plants, these domains are encoded
in distinct subunits forming heteromeric complexes. Distinctively, cytosolic ACCs from eukaryotes and
plastids of graminaceous monocots, are organized in a single multidomain polypeptide. Until now, no
multidomain ACCs had been discovered in bacteria. Here, we show that a putative multidomain ACC
in Saccharopolyspora erythraea is encoded by the sace_4237 gene, representing the frst prokaryotic
ACC homodimeric multidomain complex described. The SACE_4237 complex has both acetyl-CoA and
propionyl-CoA carboxylase activities. Importantly, we demonstrate that sace_4237 is essential for S.
erythraea survival as determined by the construction of a sace_4237 conditional mutant. Altogether,
our results show that this prokaryotic homodimeric multidomain ACC provides malonyl-CoA for de novo
fatty acid biosynthesis. Furthermore, the data presented here suggests that evolution of these enzyme
complexes, from single domain subunits to eukaryotic multidomain ACCs, occurred in bacteria through
domain fusion.
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