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  1. Article: Evolving a New Efficient Mode of Fructose Utilization for Improved Bioproduction in

    Krahn, Irene / Bonder, Daniel / Torregrosa-Barragán, Lucía / Stoppel, Dominik / Krause, Jens P / Rosenfeldt, Natalie / Meiswinkel, Tobias M / Seibold, Gerd M / Wendisch, Volker F / Lindner, Steffen N

    Frontiers in bioengineering and biotechnology

    2021  Volume 9, Page(s) 669093

    Abstract: Fructose utilization ... ...

    Abstract Fructose utilization in
    Language English
    Publishing date 2021-05-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2719493-0
    ISSN 2296-4185
    ISSN 2296-4185
    DOI 10.3389/fbioe.2021.669093
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Regulation of the malic enzyme gene malE by the transcriptional regulator MalR in Corynebacterium glutamicum.

    Krause, Jens P / Polen, Tino / Youn, Jung-Won / Emer, Denise / Eikmanns, Bernhard J / Wendisch, Volker F

    Journal of biotechnology

    2012  Volume 159, Issue 3, Page(s) 204–215

    Abstract: Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC ... ...

    Abstract Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC 13032, which is known to involve the nitrogen regulator AmtR. Gel shift experiments using purified regulators RamA and RamB revealed binding of these regulators to the malE promoter. In DNA-affinity purification experiments a hitherto uncharacterized transcriptional regulator belonging to the MarR family was found to bind to malE promoter DNA and was designated as MalR. C. glutamicum cells overexpressing malR showed reduced MalE activities in LB medium or in minimal media with acetate, glucose, pyruvate or citrate. Deletion of malR positively affected MalE activities during growth in LB medium and minimal media with pyruvate, glucose or the TCA cycle dicarboxylates l-malate, succinate and fumarate. Transcriptional fusion analysis revealed elevated malE promoter activity in the malR deletion mutant during growth in pyruvate minimal medium suggesting that MalR acts as a repressor of malE. Purified MalR bound malE promoter DNA in gel shift experiments. Two MalR binding sites were identified in the malE promoter by mutational analysis. Thus, MalR contributes to the complex transcriptional control of malE which also involves RamA, RamB and AmtR.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Sequence ; Consensus Sequence ; Corynebacterium glutamicum/enzymology ; Corynebacterium glutamicum/genetics ; Malate Dehydrogenase/genetics ; Malate Dehydrogenase/metabolism ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Binding ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Sequence Deletion ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic/genetics
    Chemical Substances Bacterial Proteins ; Repressor Proteins ; Transcription Factors ; malR protein, bacteria ; Malate Dehydrogenase (EC 1.1.1.37)
    Language English
    Publishing date 2012-06-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 843647-2
    ISSN 1873-4863 ; 0168-1656 ; 1389-0352
    ISSN (online) 1873-4863
    ISSN 0168-1656 ; 1389-0352
    DOI 10.1016/j.jbiotec.2012.01.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2299: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  3. Article ; Online: Establishment of cyanophycin biosynthesis in Pichia pastoris and optimization by use of engineered cyanophycin synthetases.

    Steinle, Anna / Witthoff, Sabrina / Krause, Jens P / Steinbüchel, Alexander

    Applied and environmental microbiology

    2009  Volume 76, Issue 4, Page(s) 1062–1070

    Abstract: Two strains of the methylotrophic yeast Pichia pastoris were used to establish cyanophycin (multi-L-arginyl-poly-L-aspartic acid [CGP]) synthesis and to explore the applicability of this industrially widely used microorganism for the production of this ... ...

    Abstract Two strains of the methylotrophic yeast Pichia pastoris were used to establish cyanophycin (multi-L-arginyl-poly-L-aspartic acid [CGP]) synthesis and to explore the applicability of this industrially widely used microorganism for the production of this polyamide. Therefore, the CGP synthetase gene from the cyanobacterium Synechocystis sp. strain PCC 6308 (cphA(6308)) was expressed under the control of the alcohol oxidase 1 promoter, yielding CGP contents of up to 10.4% (wt/wt), with the main fraction consisting of the soluble form of the polymer. To increase the polymer contents and to obtain further insights into the structural or catalytic properties of the enzyme, site-directed mutagenesis was applied to cphA(6308) and the mutated gene products were analyzed after expression in P. pastoris and Escherichia coli, respectively. CphA(6308)Delta1, which was truncated by one amino acid at the C terminus; point mutated CphA(6308)C595S; and the combined double-mutant CphA(6308)Delta1C595S protein were purified. They exhibited up to 2.5-fold higher enzyme activities of 4.95 U/mg, 3.20 U/mg, and 4.17 U/mg, respectively, than wild-type CphA(6308) (2.01 U/mg). On the other hand, CphA proteins truncated by two (CphA(6308)Delta2) or three (CphA(6308)Delta3) amino acids at the C terminus showed similar or reduced CphA enzyme activity in comparison to CphA(6308). In flask experiments, a maximum of 14.3% (wt/wt) CGP was detected after the expression of CphA(6308)Delta1 in P. pastoris. For stabilization of the expression plasmid, the his4 gene from Saccharomyces cerevisiae was cloned into the expression vector used and the constructs were transferred to histidine auxotrophic P. pastoris strain GS115. Parallel fermentations at a one-to-one scale revealed 26 degrees C and 6.0 as the optimal temperature and pH, respectively, for CGP synthesis. After optimization of fermentation parameters, medium composition, and the length of the cultivation period, CGP contents could be increased from 3.2 to 13.0% (wt/wt) in cells of P. pastoris GS115 expressing CphA(6308) and up to even 23.3% (wt/wt) in cells of P. pastoris GS115 expressing CphA(6308)Delta1.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant/genetics ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Fermentation ; Genes, Bacterial ; Hydrogen-Ion Concentration ; Kinetics ; Mutagenesis, Site-Directed ; Peptide Synthases/chemistry ; Peptide Synthases/genetics ; Peptide Synthases/metabolism ; Pichia/genetics ; Pichia/growth & development ; Pichia/metabolism ; Plant Proteins/biosynthesis ; Protein Engineering ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Synechocystis/enzymology ; Synechocystis/genetics ; Temperature
    Chemical Substances Bacterial Proteins ; DNA, Recombinant ; Plant Proteins ; Recombinant Proteins ; cyanophycin ; Peptide Synthases (EC 6.3.2.-) ; cyanophycin synthase, bacteria (EC 6.3.2.-)
    Language English
    Publishing date 2009-12-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.01659-09
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 201: Show issues Location:
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  4. Article: Establishment of Cyanophycin Biosynthesis in Pichia pastoris and Optimization by Use of Engineered Cyanophycin Synthetases

    Steinle, Anna / Witthoff, Sabrina / Krause, Jens P / Steinbüchel, Alexander

    Applied and environmental microbiology. 2010 Feb. 15, v. 76, no. 4

    2010  

    Abstract: Two strains of the methylotrophic yeast Pichia pastoris were used to establish cyanophycin (multi-L-arginyl-poly-L-aspartic acid [CGP]) synthesis and to explore the applicability of this industrially widely used microorganism for the production of this ... ...

    Abstract Two strains of the methylotrophic yeast Pichia pastoris were used to establish cyanophycin (multi-L-arginyl-poly-L-aspartic acid [CGP]) synthesis and to explore the applicability of this industrially widely used microorganism for the production of this polyamide. Therefore, the CGP synthetase gene from the cyanobacterium Synechocystis sp. strain PCC 6308 (cphA6308) was expressed under the control of the alcohol oxidase 1 promoter, yielding CGP contents of up to 10.4% (wt/wt), with the main fraction consisting of the soluble form of the polymer. To increase the polymer contents and to obtain further insights into the structural or catalytic properties of the enzyme, site-directed mutagenesis was applied to cphA6308 and the mutated gene products were analyzed after expression in P. pastoris and Escherichia coli, respectively. CphA6308Δ1, which was truncated by one amino acid at the C terminus; point mutated CphA6308C595S; and the combined double-mutant CphA6308Δ1C595S protein were purified. They exhibited up to 2.5-fold higher enzyme activities of 4.95 U/mg, 3.20 U/mg, and 4.17 U/mg, respectively, than wild-type CphA6308 (2.01 U/mg). On the other hand, CphA proteins truncated by two (CphA6308Δ2) or three (CphA6308Δ3) amino acids at the C terminus showed similar or reduced CphA enzyme activity in comparison to CphA6308. In flask experiments, a maximum of 14.3% (wt/wt) CGP was detected after the expression of CphA6308Δ1 in P. pastoris. For stabilization of the expression plasmid, the his4 gene from Saccharomyces cerevisiae was cloned into the expression vector used and the constructs were transferred to histidine auxotrophic P. pastoris strain GS115. Parallel fermentations at a one-to-one scale revealed 26°C and 6.0 as the optimal temperature and pH, respectively, for CGP synthesis. After optimization of fermentation parameters, medium composition, and the length of the cultivation period, CGP contents could be increased from 3.2 to 13.0% (wt/wt) in cells of P. pastoris GS115 expressing CphA6308 and up to even 23.3% (wt/wt) in cells of P. pastoris GS115 expressing CphA6308Δ1.
    Keywords temperature ; proteins ; fermentation ; biosynthesis ; Komagataella pastoris ; Synechocystis ; yeasts ; acids ; Saccharomyces cerevisiae ; ligases ; genes ; pH ; polymers ; site-directed mutagenesis ; enzyme activity ; genetic vectors ; histidine ; Escherichia coli
    Language English
    Dates of publication 2010-0215
    Size p. 1062-1070.
    Publishing place American Society for Microbiology
    Document type Article
    Note Includes references ; 2019-12-05
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.01659-09
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2498: Show issues

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  5. Article: Regulation of the malic enzyme gene malE by the transcriptional regulator MalR in Corynebacterium glutamicum

    Krause, Jens P / Polen, Tino / Youn, Jung-Won / Emer, Denise / Eikmanns, Bernhard J / Wendisch, Volker F

    Journal of biotechnology. 2012 June 15, v. 159, no. 3

    2012  

    Abstract: Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC ... ...

    Abstract Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC 13032, which is known to involve the nitrogen regulator AmtR. Gel shift experiments using purified regulators RamA and RamB revealed binding of these regulators to the malE promoter. In DNA-affinity purification experiments a hitherto uncharacterized transcriptional regulator belonging to the MarR family was found to bind to malE promoter DNA and was designated as MalR. C. glutamicum cells overexpressing malR showed reduced MalE activities in LB medium or in minimal media with acetate, glucose, pyruvate or citrate. Deletion of malR positively affected MalE activities during growth in LB medium and minimal media with pyruvate, glucose or the TCA cycle dicarboxylates l-malate, succinate and fumarate. Transcriptional fusion analysis revealed elevated malE promoter activity in the malR deletion mutant during growth in pyruvate minimal medium suggesting that MalR acts as a repressor of malE. Purified MalR bound malE promoter DNA in gel shift experiments. Two MalR binding sites were identified in the malE promoter by mutational analysis. Thus, MalR contributes to the complex transcriptional control of malE which also involves RamA, RamB and AmtR.
    Keywords Corynebacterium glutamicum ; DNA ; acetates ; amino acids ; bacteria ; binding sites ; biotechnology ; citrates ; gels ; genes ; glucose ; malic enzyme ; mutants ; nitrogen ; pyruvic acid ; succinic acid ; transcription (genetics) ; transcription factors ; tricarboxylic acid cycle
    Language English
    Dates of publication 2012-0615
    Size p. 204-215.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 843647-2
    ISSN 1873-4863 ; 0168-1656 ; 1389-0352
    ISSN (online) 1873-4863
    ISSN 0168-1656 ; 1389-0352
    DOI 10.1016/j.jbiotec.2012.01.003
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2299: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article: Regulation of the malic enzyme gene malE by the transcriptional regulator MalR in Corynebacterium glutamicum

    Krause, Jens P. / Polen, Tino / Youn, Jung-Won / Emer, Denise / Eikmanns, Bernhard J. / Wendisch, Volker F.

    Journal of biotechnology

    Volume v. 159,, Issue no. 3

    Abstract: Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC ... ...

    Abstract Corynebacterium glutamicum is a Gram-positive nonpathogenic bacterium that is used for the biotechnological production of amino acids. Here, we investigated the transcriptional control of the malE gene encoding malic enzyme (MalE) in C. glutamicum ATCC 13032, which is known to involve the nitrogen regulator AmtR. Gel shift experiments using purified regulators RamA and RamB revealed binding of these regulators to the malE promoter. In DNA-affinity purification experiments a hitherto uncharacterized transcriptional regulator belonging to the MarR family was found to bind to malE promoter DNA and was designated as MalR. C. glutamicum cells overexpressing malR showed reduced MalE activities in LB medium or in minimal media with acetate, glucose, pyruvate or citrate. Deletion of malR positively affected MalE activities during growth in LB medium and minimal media with pyruvate, glucose or the TCA cycle dicarboxylates l-malate, succinate and fumarate. Transcriptional fusion analysis revealed elevated malE promoter activity in the malR deletion mutant during growth in pyruvate minimal medium suggesting that MalR acts as a repressor of malE. Purified MalR bound malE promoter DNA in gel shift experiments. Two MalR binding sites were identified in the malE promoter by mutational analysis. Thus, MalR contributes to the complex transcriptional control of malE which also involves RamA, RamB and AmtR.
    Keywords acetates ; tricarboxylic acid cycle ; binding sites ; genes ; transcription factors ; transcription (genetics) ; malic enzyme ; gels ; nitrogen ; mutants ; pyruvic acid ; Corynebacterium glutamicum ; biotechnology ; succinic acid ; amino acids ; citrates ; bacteria ; glucose ; DNA
    Language English
    Document type Article
    ISSN 0168-1656
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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