한빛사논문
So-Hee Son1,2,7, Jae-Eung Kim1,7, Gyuri Park3, Young-Joon Ko1, Bong Hyun Sung4, Jongcheol Seo5, Seung Soo Oh2,3,6,* & Ju Young Lee1,*
1Research Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology (KRICT), 406-30, Jongga-ro, Jung-gu, Ulsan 44429, Republic of Korea. 2School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology (POSTECH), Pohang, Gyeongbuk 37673, Republic of Korea. 3Department of Materials Science and Engineering, Pohang University of Science and Technology (POSTECH), Pohang, Gyeongbuk 37673, Republic of Korea. 4Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea. 5Department of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang, Gyeongbuk 37673, Republic of Korea. 6Institute for Convergence Research and Education in Advanced Technology (I-CREATE), Yonsei University, Incheon 21983, Republic of Korea. 7These authors contributed equally: So-Hee Son, Jae-Eung Kim.
*Corresponding author.
Abstract
Metabolites are often unable to permeate cell membranes and are thus accumulated inside cells. We investigate whether engineered microbes can exclusively secrete intracellular metabolites because sustainable metabolite secretion holds a great potential for mass-production of high-value chemicals in an efficient and continuous manner. In this study, we demonstrate a synthetic pathway for a metabolite trafficking system that enables lipophilic terpene secretion by yeast cells. When metabolite-binding proteins are tagged with signal peptides, metabolite trafficking is highly achievable; loaded metabolites can be precisely delivered to a desired location within or outside the cell. As a proof of concept, we systematically couple a terpene-binding protein with an export signal peptide and subsequently demonstrate efficient, yet selective terpene secretion by yeast (~225 mg/L for squalene and ~1.6 mg/L for β-carotene). Other carrier proteins can also be readily fused with desired signal peptides, thereby tailoring different metabolite trafficking pathways in different microbes. To the best of our knowledge, this is the most efficient cognate pathway for metabolite secretion by microorganisms.
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