Production of stable isotope labelled lipase Lip2 from Yarrowia lipolytica for NMR: Investigation of several expression systems
•Yarrowia lipolytica, Pichia pastoris, Escherichia coli and cell free expression were tested.•Yarrowia lipolytica was the most efficient system for production of 15N labelled Lip2.•First 15N–1H HSQC spectra of Lip2 was recorded. Extracellular lipase Lip2 from Yarrowia lipolytica is a promising bioca...
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| Published in | Protein expression and purification Vol. 101; pp. 14 - 20 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
01.09.2014
Elsevier |
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| Abstract | •Yarrowia lipolytica, Pichia pastoris, Escherichia coli and cell free expression were tested.•Yarrowia lipolytica was the most efficient system for production of 15N labelled Lip2.•First 15N–1H HSQC spectra of Lip2 was recorded.
Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia coli, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring 15N–1H HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR. |
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| AbstractList | Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia colt, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring N-15-H-1 HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR. (C) 20114 Published by Elsevier Inc. Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia coli, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring (15)N-(1)H HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR.Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia coli, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring (15)N-(1)H HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR. •Yarrowia lipolytica, Pichia pastoris, Escherichia coli and cell free expression were tested.•Yarrowia lipolytica was the most efficient system for production of 15N labelled Lip2.•First 15N–1H HSQC spectra of Lip2 was recorded. Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia coli, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring 15N–1H HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR. Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These features comprise a mobile domain called the lid that controls access to the catalytic site. Conformational rearrangements of the lid have been suggested to regulate lipase enzymatic activities. We used nuclear magnetic resonance to investigate the dynamics of Lip2 by exploring four expression systems, Escherichia coli, cell-free, Pichia pastoris and Y. lipolytica to produce uniformly labelled enzyme. The expression of Lip2 was assessed by determining its specific activity and measuring (15)N-(1)H HSQC spectra. Y. lipolytica turned out to be the most efficient expression system. Here, we report the first use of Y. lipolytica as an expression host for the production of uniform stable isotopic labelled protein for further structural and dynamics studies using NMR. |
| Author | Remaud-Siméon, M. Nars, G. André, I. Saurel, O. Marty, A. Bordes, F. Saves, I. Milon, A. |
| Author_xml | – sequence: 1 givenname: G. surname: Nars fullname: Nars, G. organization: Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France – sequence: 2 givenname: O. surname: Saurel fullname: Saurel, O. organization: CNRS, IPBS UMR 5089, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, BP 64182, F-31077 Toulouse Cedex 04, France – sequence: 3 givenname: F. surname: Bordes fullname: Bordes, F. organization: Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France – sequence: 4 givenname: I. surname: Saves fullname: Saves, I. organization: CNRS, IPBS UMR 5089, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, BP 64182, F-31077 Toulouse Cedex 04, France – sequence: 5 givenname: M. surname: Remaud-Siméon fullname: Remaud-Siméon, M. organization: Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France – sequence: 6 givenname: I. surname: André fullname: André, I. organization: Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France – sequence: 7 givenname: A. surname: Milon fullname: Milon, A. organization: CNRS, IPBS UMR 5089, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, BP 64182, F-31077 Toulouse Cedex 04, France – sequence: 8 givenname: A. surname: Marty fullname: Marty, A. email: alain.marty@insa-toulouse.fr organization: Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France |
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| Keywords | Yarrowia lipolytica lipase lip2 Cell-free Yeast Pichia pastoris Isotope labelling Yarrowia lipolytica HETEROLOGOUS PROTEIN EXPRESSION CELLS QUANTITIES ENANTIOSELECTIVITY YEAST PICHIA-PASTORIS RECOMBINANT PURIFICATION DYNAMICS BINDING ACID-ESTERS |
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| Snippet | •Yarrowia lipolytica, Pichia pastoris, Escherichia coli and cell free expression were tested.•Yarrowia lipolytica was the most efficient system for production... Extracellular lipase Lip2 from Yarrowia lipolytica is a promising biocatalyst with unusual structural features, as indicated by X-ray crystallography. These... |
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| SubjectTerms | Catalytic Domain Cell-free Cell-Free System - metabolism Chemical and Process Engineering Crystallography, X-Ray Engineering Sciences Escherichia coli - genetics Escherichia coli - metabolism Food engineering Fungal Proteins - biosynthesis Fungal Proteins - chemistry Fungal Proteins - genetics Gene Expression - genetics Isotope Labeling - methods Isotope labelling Life Sciences Lipase - biosynthesis Lipase - chemistry Lipase - genetics Nuclear Magnetic Resonance, Biomolecular Pichia - genetics Pichia - metabolism Pichia pastoris Yarrowia - enzymology Yarrowia - genetics Yarrowia - metabolism Yarrowia lipolytica Yarrowia lipolytica lipase lip2 Yeast |
| Title | Production of stable isotope labelled lipase Lip2 from Yarrowia lipolytica for NMR: Investigation of several expression systems |
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