Journal
FRONTIERS IN MICROBIOLOGY
Volume 9, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2018.00047
Keywords
malonyl-CoA sensor; phosphorylation site mutations; acetyl-CoA carboxylase; 3-hydroxypropionic acid; Saccharomyces cerevisiae
Categories
Funding
- National Natural Science Foundation of China [31770101, 31470163, 31711530155]
- Key R&D Program of Shandong Province [2017GSF21110, 2015GSF121015]
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Malonyl-coenzyme A (malonyl-CoA) is a critical precursor for the biosynthesis of a variety of biochemicals. It is synthesized by the catalysis of acetyl-CoA carboxylase (Acc1p), which was demonstrated to be deactivated by the phosphorylation of Snf1 protein kinase in yeast. In this study, we designed a synthetic malonyl-CoA biosensor and used it to screen phosphorylation site mutations of Acc1p in Saccharomyces cerevisiae. Thirteen phosphorylation sites were mutated, and a combination of three site mutations in Acc1p, S686A, S659A, and S1157A, was found to increase malonyl-CoA availability. ACC1(S686AS659AS1157A) expression also improved the production of 3-hydroxypropionic acid, a malonyl-CoA-derived chemical, compared to both wild type and the previously reported ACC1(S659AS1157A) mutation. This mutation will also be beneficial for other malonyl-CoA-derived products.
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