Reversible Chemoenzymatic Protein Labeling
Researchers at UC San Diego have developed a method to reversibly tag a protein essential for the assembly of complex molecules in biological cells. Specifically, the inventors have invented new methods and compositions for removing a phosphopantethiene analogue moiety from an ACP-phosphopantetheine conjugate thereby providing Apo-ACP proteins. This reversible process can be repeated multiple times without degradation in protein identity, making it a major addition to an already popular and useful labeling method. The technique could help researchers to rewire cellular factories, such as those involved in nonribosomal protein, and fatty acid syntheses, to allow construction of new products, such as biofuels or drugs. Given the multitude of existing opportunities for ACP labeling, particularly in work involving fusion-protein applications and natural-product biosynthetic studies, this reversible methodology will provide markedly improved flexibility for rapid modification of protein species. Additionally, the cost-saving measure of recovering valuable apo-ACP substrates cannot be overlooked.
Inventor: BURKART, Michael D. | KOSA, Nicolas M. | HAUSHALTER, Robert W.
Priority Number: WO2014043561A1
IPC Current: C07K001900 | C07F000909 | C07F000936
Assignee Applicant: The Regents of the University of California
Title: REVERSIBLE CHEMOENZYMATIC LABELING OF NATIVE AND FUSION CARRIER PROTEIN MOTIFS | MARQUAGE CHIMIO-ENZYMATIQUE RÉVERSIBLE DE MOTIFS DE PROTÉINE DE SUPPORT NATIVE ET DE FUSION
Usefulness: REVERSIBLE CHEMOENZYMATIC LABELING OF NATIVE AND FUSION CARRIER PROTEIN MOTIFS | MARQUAGE CHIMIO-ENZYMATIQUE RÉVERSIBLE DE MOTIFS DE PROTÉINE DE SUPPORT NATIVE ET DE FUSION
Summary: The method is useful for forming an apo-ACP from an ACP-phosphopantetheine conjugate (claimed).
Novelty: Forming apolipoprotein-acyl carrier proteins from acyl carrier proteins-phosphopantetheine conjugate involves contacting conjugate with acyl carrier proteins hydrolase and allowing hydrolase to cleave phosphodiester linker
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State Of Development The researchers have published on the full reversibility of the technique in visualization and functional studies. Results indicate that given the wide substrate acceptance demonstrated by this enzymatic approach, various fluorescent and functional tags can be exchanged on a single protein with robustness not offered by previous enzymatic methods. Intellectual Property Info This technology is available for worldwide licensing. Related Materials Nicolas M Kosa, Robert W Haushalter, Andrew R Smith & Michael D Burkart “Reversible labeling of native and fusion-protein motifs” Nature Methods 9, 2012, pp 981-984. Additional Technologies by these Inventors Tech ID/UC Case 23288/2013-030-0 Related Cases 2013-030-0
Coverage in Sept 19, 2012 issue of Chemical & Engineering News “Tool May Aid Biosynthetic Reverse Engineering”
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