Phase‐Separated Multienzyme Compartmentalization for Terpene Biosynthesis in a Prokaryote
Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the...
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Published in | Angewandte Chemie Vol. 134; no. 29 |
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Main Authors | , , , , , , , , , |
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Abstract | Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the biosynthesis of a terpene, α‐farnesene, in the prokaryote E. coli. RGGRGG derived from LAF‐1 was used as the scaffold protein to form the condensates by LLPS. Multienzyme condensates were then formed by assembling two enzymes Idi and IspA through an RIAD/RIDD interaction. Multienzyme condensates constructed inside E. coli cells compartmentalized the cytosolic space into regions of high and low enzyme density and led to a significant enhancement of α‐farnesene production. This work demonstrates LLPS‐driven compartmentalization of the cytosolic space of prokaryotic cells, condensation of a biosynthetic pathway, and enhancement of the biosynthesis of α‐farnesene.
Prokaryotic cells generally lack organelles to compartmentalize the intracellular content. When liquid–liquid phase‐separated protein condensates were constructed inside E. coli, membraneless organelles were created to compartmentalize terpene biosynthetic enzymes. Compartmentalizing the enzymes in protein condensates increased the production rate of the terpene product, showing this method to be an effective way of enhancing heterologous biosynthesis. |
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AbstractList | Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the biosynthesis of a terpene, α‐farnesene, in the prokaryote E. coli. RGGRGG derived from LAF‐1 was used as the scaffold protein to form the condensates by LLPS. Multienzyme condensates were then formed by assembling two enzymes Idi and IspA through an RIAD/RIDD interaction. Multienzyme condensates constructed inside E. coli cells compartmentalized the cytosolic space into regions of high and low enzyme density and led to a significant enhancement of α‐farnesene production. This work demonstrates LLPS‐driven compartmentalization of the cytosolic space of prokaryotic cells, condensation of a biosynthetic pathway, and enhancement of the biosynthesis of α‐farnesene. Abstract Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the biosynthesis of a terpene, α‐farnesene, in the prokaryote E. coli . RGGRGG derived from LAF‐1 was used as the scaffold protein to form the condensates by LLPS. Multienzyme condensates were then formed by assembling two enzymes Idi and IspA through an RIAD/RIDD interaction. Multienzyme condensates constructed inside E. coli cells compartmentalized the cytosolic space into regions of high and low enzyme density and led to a significant enhancement of α‐farnesene production. This work demonstrates LLPS‐driven compartmentalization of the cytosolic space of prokaryotic cells, condensation of a biosynthetic pathway, and enhancement of the biosynthesis of α‐farnesene. Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the biosynthesis of a terpene, α‐farnesene, in the prokaryote E. coli. RGGRGG derived from LAF‐1 was used as the scaffold protein to form the condensates by LLPS. Multienzyme condensates were then formed by assembling two enzymes Idi and IspA through an RIAD/RIDD interaction. Multienzyme condensates constructed inside E. coli cells compartmentalized the cytosolic space into regions of high and low enzyme density and led to a significant enhancement of α‐farnesene production. This work demonstrates LLPS‐driven compartmentalization of the cytosolic space of prokaryotic cells, condensation of a biosynthetic pathway, and enhancement of the biosynthesis of α‐farnesene. Prokaryotic cells generally lack organelles to compartmentalize the intracellular content. When liquid–liquid phase‐separated protein condensates were constructed inside E. coli, membraneless organelles were created to compartmentalize terpene biosynthetic enzymes. Compartmentalizing the enzymes in protein condensates increased the production rate of the terpene product, showing this method to be an effective way of enhancing heterologous biosynthesis. |
Author | He, Yanping Wang, Yue Wei, Qixin Wu, Wanjie Xia, Jiang Zhou, Renjie Qu, Jianan Liu, Min Gao, Jiayang Jiang, Liwen |
Author_xml | – sequence: 1 givenname: Yue surname: Wang fullname: Wang, Yue organization: The Chinese University of Hong Kong – sequence: 2 givenname: Min surname: Liu fullname: Liu, Min organization: The Chinese University of Hong Kong – sequence: 3 givenname: Qixin surname: Wei fullname: Wei, Qixin organization: The Chinese University of Hong Kong – sequence: 4 givenname: Wanjie surname: Wu fullname: Wu, Wanjie organization: Hong Kong University of Science and Technology – sequence: 5 givenname: Yanping surname: He fullname: He, Yanping organization: The Chinese University of Hong Kong – sequence: 6 givenname: Jiayang surname: Gao fullname: Gao, Jiayang organization: The Chinese University of Hong Kong – sequence: 7 givenname: Renjie surname: Zhou fullname: Zhou, Renjie organization: The Chinese University of Hong Kong – sequence: 8 givenname: Liwen surname: Jiang fullname: Jiang, Liwen organization: The Chinese University of Hong Kong – sequence: 9 givenname: Jianan surname: Qu fullname: Qu, Jianan organization: Hong Kong University of Science and Technology – sequence: 10 givenname: Jiang orcidid: 0000-0001-8112-7625 surname: Xia fullname: Xia, Jiang email: jiangxia@cuhk.edu.hk organization: The Chinese University of Hong Kong |
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Snippet | Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular... Abstract Liquid–liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase‐separated subcellular... |
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SubjectTerms | Biosynthesis Chemistry Cofactors Condensates E coli Enzymes Farnesene Liquid phases Multienzyme Catalysis Multienzyme Compartmentalization Phase Separation Substrates Terpene Biosynthesis α-Farnesene |
Title | Phase‐Separated Multienzyme Compartmentalization for Terpene Biosynthesis in a Prokaryote |
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