Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli
Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demon...
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| Veröffentlicht in: | Biotechnology letters 2007-10, Vol.29 (10), p.1513-1518 |
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| container_title | Biotechnology letters |
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| creator | Park, Jin-Seung Han, Kyung-Yeon Song, Jong-Am Ahn, Keum-Young Seo, Hyuk-Seong Lee, Jeewon |
| description | Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries. |
| doi_str_mv | 10.1007/s10529-007-9417-3 |
| format | Article |
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We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-007-9417-3</identifier><identifier>PMID: 17549433</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Springer Netherlands</publisher><subject>Biological and medical sciences ; Biotechnology ; Dehydrogenase ; E coli ; Electrophoresis, Gel, Two-Dimensional ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Escherichia coli proteome ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Bacterial ; Hot Temperature ; malate dehydrogenase ; Malate Dehydrogenase - genetics ; Malate Dehydrogenase - metabolism ; Protein Folding ; Proteins ; Pseudomonas putida ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Solubility ; Solubility enhancer ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; stress response</subject><ispartof>Biotechnology letters, 2007-10, Vol.29 (10), p.1513-1518</ispartof><rights>2007 INIST-CNRS</rights><rights>Springer Science+Business Media B.V. 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-c3185f4b93fed3881fcaf0dac199edf54d0b34fed3ddeda3c417b8b8e8b7eee13</citedby><cites>FETCH-LOGICAL-c443t-c3185f4b93fed3881fcaf0dac199edf54d0b34fed3ddeda3c417b8b8e8b7eee13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19040778$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17549433$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Jin-Seung</creatorcontrib><creatorcontrib>Han, Kyung-Yeon</creatorcontrib><creatorcontrib>Song, Jong-Am</creatorcontrib><creatorcontrib>Ahn, Keum-Young</creatorcontrib><creatorcontrib>Seo, Hyuk-Seong</creatorcontrib><creatorcontrib>Lee, Jeewon</creatorcontrib><title>Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><description>Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Dehydrogenase</subject><subject>E coli</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Escherichia coli proteome</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Hot Temperature</subject><subject>malate dehydrogenase</subject><subject>Malate Dehydrogenase - genetics</subject><subject>Malate Dehydrogenase - metabolism</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Pseudomonas putida</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Solubility</subject><subject>Solubility enhancer</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>stress response</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkt-LFSEUx4co2tvWH9BLSVC9NHW8OqM-xrL9gIUeap_F0eMdF--46Uxwoz8-h3thYR8KQQ_6Oed89WvTPKfwngKID4VCt1VtDVvFqWjZg2ZDO8HaXoj-YbMBymnbcbU9a56UcgMASoB43JxRUXc5Y5vmz2WxI-Zgx2CITTGQvYlmRuJwPLicdjiZgu-IIVP6hZGUFJchxDAfCE6jmSxm4lMmI86YU0y7tBRym9OMYSqkHKZ5xBJ-oyNhIvd7PW0eeRMLPjut5831p8sfF1_aq2-fv158vGot52xuLaOy83xQzKNjUlJvjQdnLFUKne-4g4Hx9cw5dIbZ-haDHCTKQSAiZefN22PdKuzngmXW-1AsxmgmrHq14KwO0bFKvvkn2UsqFfTqvyBVQgoOfQVf3QNv0pKnel0tGJc9rVOF6BGyOZWS0evbHPYmHzQFvVqtj1brNVyt1qvUF6fCy7BHd5dx8rYCr0-AKdZEn6tbodxxCjgIsTZ_eeS8SdrscmWuv2-BMgAJ9Qsx9hcLCr1l</recordid><startdate>20071001</startdate><enddate>20071001</enddate><creator>Park, Jin-Seung</creator><creator>Han, Kyung-Yeon</creator><creator>Song, Jong-Am</creator><creator>Ahn, Keum-Young</creator><creator>Seo, Hyuk-Seong</creator><creator>Lee, Jeewon</creator><general>Dordrecht : Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>20071001</creationdate><title>Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli</title><author>Park, Jin-Seung ; Han, Kyung-Yeon ; Song, Jong-Am ; Ahn, Keum-Young ; Seo, Hyuk-Seong ; Lee, Jeewon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-c3185f4b93fed3881fcaf0dac199edf54d0b34fed3ddeda3c417b8b8e8b7eee13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Dehydrogenase</topic><topic>E coli</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Escherichia coli proteome</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Hot Temperature</topic><topic>malate dehydrogenase</topic><topic>Malate Dehydrogenase - genetics</topic><topic>Malate Dehydrogenase - metabolism</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Pseudomonas putida</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Solubility</topic><topic>Solubility enhancer</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>stress response</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Jin-Seung</creatorcontrib><creatorcontrib>Han, Kyung-Yeon</creatorcontrib><creatorcontrib>Song, Jong-Am</creatorcontrib><creatorcontrib>Ahn, Keum-Young</creatorcontrib><creatorcontrib>Seo, Hyuk-Seong</creatorcontrib><creatorcontrib>Lee, Jeewon</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Jin-Seung</au><au>Han, Kyung-Yeon</au><au>Song, Jong-Am</au><au>Ahn, Keum-Young</au><au>Seo, Hyuk-Seong</au><au>Lee, Jeewon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli</atitle><jtitle>Biotechnology letters</jtitle><addtitle>Biotechnol Lett</addtitle><date>2007-10-01</date><risdate>2007</risdate><volume>29</volume><issue>10</issue><spage>1513</spage><epage>1518</epage><pages>1513-1518</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.</abstract><cop>Dordrecht</cop><pub>Dordrecht : Springer Netherlands</pub><pmid>17549433</pmid><doi>10.1007/s10529-007-9417-3</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Biological and medical sciences Biotechnology Dehydrogenase E coli Electrophoresis, Gel, Two-Dimensional Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Escherichia coli proteome Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Hot Temperature malate dehydrogenase Malate Dehydrogenase - genetics Malate Dehydrogenase - metabolism Protein Folding Proteins Pseudomonas putida Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Solubility Solubility enhancer Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization stress response |
| title | Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli |
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