Directed evolution of the transcription factor XylS for development of improved expression systems
Summary The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimul...
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Published in | Microbial biotechnology Vol. 3; no. 1; pp. 38 - 47 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Publishing Ltd
01.01.2010
John Wiley & Sons, Inc |
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Abstract | Summary
The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimulate transcription in Escherichia coli from Pm. A first round of mutagenesis using error‐prone PCR on xylS was used to construct a library consisting of about 430 000 clones, and this library could be efficiently screened with respect to stimulation of expression from Pm due to a positive correlation between the level of expression of the reporter gene, bla (encoding β‐lactamase), and the ampicillin tolerance of the corresponding host cells. Fourteen different amino acid substitutions in XylS were found to separately lead to up to nearly a threefold stimulation of expression under induced conditions, relative to wild type. These mutations were all located in the part corresponding to the N‐terminal half of the protein. Varying combinations of the mutations resulted in further stimulation, and the best results (about 10‐fold stimulation under induced conditions) were obtained by using a random shuffling procedure followed by a new round of screening. The uninduced levels of expression for the same mutants also increased, but only about four times. Through in silico 3D modelling of the N‐terminal domain of XylS, it was observed that the evolved mutant proteins contained substitutions that were positioned in different parts of the predicted structure, including a β‐barrel putatively responsible for effector binding and a coiled coil probably important for dimerization. The total production of the host‐toxic antibody fragment scFv‐phOx expressed from Pm with the evolved XylS mutant protein StEP‐13 was about ninefold higher than with wild‐type XylS, demonstrating that directed evolution of transcription factors can be an important new tool to achieve high‐level recombinant protein production. |
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AbstractList | Summary
The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimulate transcription in Escherichia coli from Pm. A first round of mutagenesis using error‐prone PCR on xylS was used to construct a library consisting of about 430 000 clones, and this library could be efficiently screened with respect to stimulation of expression from Pm due to a positive correlation between the level of expression of the reporter gene, bla (encoding β‐lactamase), and the ampicillin tolerance of the corresponding host cells. Fourteen different amino acid substitutions in XylS were found to separately lead to up to nearly a threefold stimulation of expression under induced conditions, relative to wild type. These mutations were all located in the part corresponding to the N‐terminal half of the protein. Varying combinations of the mutations resulted in further stimulation, and the best results (about 10‐fold stimulation under induced conditions) were obtained by using a random shuffling procedure followed by a new round of screening. The uninduced levels of expression for the same mutants also increased, but only about four times. Through in silico 3D modelling of the N‐terminal domain of XylS, it was observed that the evolved mutant proteins contained substitutions that were positioned in different parts of the predicted structure, including a β‐barrel putatively responsible for effector binding and a coiled coil probably important for dimerization. The total production of the host‐toxic antibody fragment scFv‐phOx expressed from Pm with the evolved XylS mutant protein StEP‐13 was about ninefold higher than with wild‐type XylS, demonstrating that directed evolution of transcription factors can be an important new tool to achieve high‐level recombinant protein production. The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimulate transcription in Escherichia coli from Pm. A first round of mutagenesis using error-prone PCR on xylS was used to construct a library consisting of about 430,000 clones, and this library could be efficiently screened with respect to stimulation of expression from Pm due to a positive correlation between the level of expression of the reporter gene, bla (encoding β-lactamase), and the ampicillin tolerance of the corresponding host cells. Fourteen different amino acid substitutions in XylS were found to separately lead to up to nearly a threefold stimulation of expression under induced conditions, relative to wild type. These mutations were all located in the part corresponding to the N-terminal half of the protein. Varying combinations of the mutations resulted in further stimulation, and the best results (about 10-fold stimulation under induced conditions) were obtained by using a random shuffling procedure followed by a new round of screening. The uninduced levels of expression for the same mutants also increased, but only about four times. Through in silico 3D modelling of the N-terminal domain of XylS, it was observed that the evolved mutant proteins contained substitutions that were positioned in different parts of the predicted structure, including a β-barrel putatively responsible for effector binding and a coiled coil probably important for dimerization. The total production of the host-toxic antibody fragment scFv-phOx expressed from Pm with the evolved XylS mutant protein StEP-13 was about ninefold higher than with wild-type XylS, demonstrating that directed evolution of transcription factors can be an important new tool to achieve high-level recombinant protein production. Summary The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimulate transcription in Escherichia coli from Pm. A first round of mutagenesis using error‐prone PCR on xylS was used to construct a library consisting of about 430 000 clones, and this library could be efficiently screened with respect to stimulation of expression from Pm due to a positive correlation between the level of expression of the reporter gene, bla (encoding β‐lactamase), and the ampicillin tolerance of the corresponding host cells. Fourteen different amino acid substitutions in XylS were found to separately lead to up to nearly a threefold stimulation of expression under induced conditions, relative to wild type. These mutations were all located in the part corresponding to the N‐terminal half of the protein. Varying combinations of the mutations resulted in further stimulation, and the best results (about 10‐fold stimulation under induced conditions) were obtained by using a random shuffling procedure followed by a new round of screening. The uninduced levels of expression for the same mutants also increased, but only about four times. Through in silico 3D modelling of the N‐terminal domain of XylS, it was observed that the evolved mutant proteins contained substitutions that were positioned in different parts of the predicted structure, including a β‐barrel putatively responsible for effector binding and a coiled coil probably important for dimerization. The total production of the host‐toxic antibody fragment scFv‐phOx expressed from Pm with the evolved XylS mutant protein StEP‐13 was about ninefold higher than with wild‐type XylS, demonstrating that directed evolution of transcription factors can be an important new tool to achieve high‐level recombinant protein production. The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under high cell density conditions. Here we report directed evolution of XylS resulting in mutant proteins with increased ability to stimulate transcription in Escherichia coli from Pm. A first round of mutagenesis using error‐prone PCR on xylS was used to construct a library consisting of about 430 000 clones, and this library could be efficiently screened with respect to stimulation of expression from Pm due to a positive correlation between the level of expression of the reporter gene, bla (encoding β‐lactamase), and the ampicillin tolerance of the corresponding host cells. Fourteen different amino acid substitutions in XylS were found to separately lead to up to nearly a threefold stimulation of expression under induced conditions, relative to wild type. These mutations were all located in the part corresponding to the N‐terminal half of the protein. Varying combinations of the mutations resulted in further stimulation, and the best results (about 10‐fold stimulation under induced conditions) were obtained by using a random shuffling procedure followed by a new round of screening. The uninduced levels of expression for the same mutants also increased, but only about four times. Through in silico 3D modelling of the N‐terminal domain of XylS, it was observed that the evolved mutant proteins contained substitutions that were positioned in different parts of the predicted structure, including a β‐barrel putatively responsible for effector binding and a coiled coil probably important for dimerization. The total production of the host‐toxic antibody fragment scFv‐phOx expressed from Pm with the evolved XylS mutant protein StEP‐13 was about ninefold higher than with wild‐type XylS, demonstrating that directed evolution of transcription factors can be an important new tool to achieve high‐level recombinant protein production. |
Author | Vee Aune, Trond Erik Brautaset, Trygve Drabløs, Finn Valla, Svein Bakke, Ingrid Lale, Rahmi |
AuthorAffiliation | 1 Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway 3 SINTEF Materials and Chemistry, Department of Biotechnology, SINTEF, 7465 Trondheim, Norway 2 Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, 7006 Trondheim, Norway |
AuthorAffiliation_xml | – name: 1 Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway – name: 3 SINTEF Materials and Chemistry, Department of Biotechnology, SINTEF, 7465 Trondheim, Norway – name: 2 Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, 7006 Trondheim, Norway |
Author_xml | – sequence: 1 givenname: Trond Erik surname: Vee Aune fullname: Vee Aune, Trond Erik organization: Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 2 givenname: Ingrid surname: Bakke fullname: Bakke, Ingrid organization: Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 3 givenname: Finn surname: Drabløs fullname: Drabløs, Finn organization: Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, 7006 Trondheim, Norway – sequence: 4 givenname: Rahmi surname: Lale fullname: Lale, Rahmi organization: Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 5 givenname: Trygve surname: Brautaset fullname: Brautaset, Trygve organization: SINTEF Materials and Chemistry, Department of Biotechnology, SINTEF, 7465 Trondheim, Norway – sequence: 6 givenname: Svein surname: Valla fullname: Valla, Svein email: svein.valla@biotech.ntnu.no organization: Department of Biotechnology, Norwegian University of Science and Technology, 7491 Trondheim, Norway |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21255304$$D View this record in MEDLINE/PubMed |
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Snippet | Summary
The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein... The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under... Summary The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein... The inducible Pm promoter together with its cognate positive transcription regulator XylS has been shown to be useful for recombinant protein production under... |
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StartPage | 38 |
SubjectTerms | Amino Acid Substitution - genetics Amino acids Ampicillin Ampicillin Resistance Antibiotics Antibodies Artificial Gene Fusion beta-Lactamases - genetics beta-Lactamases - metabolism Cell density Coils Deoxyribonucleic acid Dimerization Directed evolution Directed Molecular Evolution DNA E coli Engineering Escherichia coli - genetics Evolution Gene expression Gene Expression Regulation, Bacterial Genes, Reporter Immunological tolerance Medical research Models, Molecular Mutagenesis Mutants Mutation Polymerase Chain Reaction - methods Promoter Regions, Genetic Protein Structure, Tertiary Proteins Reporter gene RNA polymerase Stimulation Three dimensional models Trans-Activators - genetics Trans-Activators - metabolism Transcription factors Transcription, Genetic |
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Title | Directed evolution of the transcription factor XylS for development of improved expression systems |
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