Overproduction of dnaJ in Escherichia coli improves in vivo solubility of the recombinant fish-derived transglutaminase
The overexpression of red sea bream (Pagrus major)transglutaminase (TGase, EC 2.3.2.13) in Escherichia coli mostly leads to the accumulation of biologically inactive enzyme. Although the solubility of the gene products could by improved by cultivation at a lower temperature (26-28 degrees C), most o...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998-06, Vol.62 (6), p.1205-1210 |
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| creator | Yokoyama, K. (Ajinomoto Co. Inc., Tokyo (Japan)) Kikuchi, Y Yasueda, H |
| description | The overexpression of red sea bream (Pagrus major)transglutaminase (TGase, EC 2.3.2.13) in Escherichia coli mostly leads to the accumulation of biologically inactive enzyme. Although the solubility of the gene products could by improved by cultivation at a lower temperature (26-28 degrees C), most of he synthesized TGase was still in the form of insoluble aggregates. The effects of overproduction of molecular chaperons on the intracellular solubility of newly produced recombinant TGase were examined. The overexpression of dnaK or groES/EL did not improve solubility. However, DnaJ greatly increased the solubility of the recombinant TGase, resulting in active enzyme in the presence of calcium ions. Co-expression of dnaK along with dnaJ further increased the content of soluble TGase. Under our experimental conditions, supplementation with both DnaJ and DnaK elevated the TGase activity in the producer cells by roughly 4-fold, compared with the control strain cultured at 30 degrees C. Thus, we found that DnaJ is important in controlling the solubility of protein overproduced in E. coli |
| doi_str_mv | 10.1271/bbb.62.1205 |
| format | Article |
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Under our experimental conditions, supplementation with both DnaJ and DnaK elevated the TGase activity in the producer cells by roughly 4-fold, compared with the control strain cultured at 30 degrees C. Thus, we found that DnaJ is important in controlling the solubility of protein overproduced in E. coli</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.62.1205</identifier><identifier>PMID: 9692205</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>AMINOTRANSFERASAS ; AMINOTRANSFERASE ; AMINOTRANSFERASES ; Animals ; Bacterial Proteins - biosynthesis ; Biological and medical sciences ; Biotechnology ; co-expression ; DnaJ ; ESCHERICHIA COLI ; Escherichia coli - metabolism ; Escherichia coli Proteins ; EXPERIMENTACION IN VIVO ; EXPERIMENTATION IN VIVO ; Fundamental and applied biological sciences. 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(Ajinomoto Co. Inc., Tokyo (Japan))</creatorcontrib><creatorcontrib>Kikuchi, Y</creatorcontrib><creatorcontrib>Yasueda, H</creatorcontrib><title>Overproduction of dnaJ in Escherichia coli improves in vivo solubility of the recombinant fish-derived transglutaminase</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The overexpression of red sea bream (Pagrus major)transglutaminase (TGase, EC 2.3.2.13) in Escherichia coli mostly leads to the accumulation of biologically inactive enzyme. Although the solubility of the gene products could by improved by cultivation at a lower temperature (26-28 degrees C), most of he synthesized TGase was still in the form of insoluble aggregates. The effects of overproduction of molecular chaperons on the intracellular solubility of newly produced recombinant TGase were examined. The overexpression of dnaK or groES/EL did not improve solubility. However, DnaJ greatly increased the solubility of the recombinant TGase, resulting in active enzyme in the presence of calcium ions. Co-expression of dnaK along with dnaJ further increased the content of soluble TGase. Under our experimental conditions, supplementation with both DnaJ and DnaK elevated the TGase activity in the producer cells by roughly 4-fold, compared with the control strain cultured at 30 degrees C. Thus, we found that DnaJ is important in controlling the solubility of protein overproduced in E. coli</description><subject>AMINOTRANSFERASAS</subject><subject>AMINOTRANSFERASE</subject><subject>AMINOTRANSFERASES</subject><subject>Animals</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>co-expression</subject><subject>DnaJ</subject><subject>ESCHERICHIA COLI</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>EXPERIMENTACION IN VIVO</subject><subject>EXPERIMENTATION IN VIVO</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>HSP40 Heat-Shock Proteins</subject><subject>IN VIVO EXPERIMENTATION</subject><subject>Methods. Procedures. 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Psychology</topic><topic>Gene Expression Regulation, Bacterial - physiology</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>HSP40 Heat-Shock Proteins</topic><topic>IN VIVO EXPERIMENTATION</topic><topic>Methods. Procedures. Technologies</topic><topic>Modification of gene expression level</topic><topic>Molecular Chaperones - biosynthesis</topic><topic>PAGRUS</topic><topic>Pagrus major</topic><topic>Perciformes - metabolism</topic><topic>Plasmids - genetics</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Solubility</topic><topic>Temperature</topic><topic>TEXTURA</topic><topic>TEXTURE</topic><topic>transglutaminase</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yokoyama, K. (Ajinomoto Co. Inc., Tokyo (Japan))</creatorcontrib><creatorcontrib>Kikuchi, Y</creatorcontrib><creatorcontrib>Yasueda, H</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>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yokoyama, K. 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The effects of overproduction of molecular chaperons on the intracellular solubility of newly produced recombinant TGase were examined. The overexpression of dnaK or groES/EL did not improve solubility. However, DnaJ greatly increased the solubility of the recombinant TGase, resulting in active enzyme in the presence of calcium ions. Co-expression of dnaK along with dnaJ further increased the content of soluble TGase. Under our experimental conditions, supplementation with both DnaJ and DnaK elevated the TGase activity in the producer cells by roughly 4-fold, compared with the control strain cultured at 30 degrees C. Thus, we found that DnaJ is important in controlling the solubility of protein overproduced in E. coli</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>9692205</pmid><doi>10.1271/bbb.62.1205</doi><tpages>6</tpages></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 1998-06, Vol.62 (6), p.1205-1210 |
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| source | J-STAGE Free; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Open Access Titles of Japan; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | AMINOTRANSFERASAS AMINOTRANSFERASE AMINOTRANSFERASES Animals Bacterial Proteins - biosynthesis Biological and medical sciences Biotechnology co-expression DnaJ ESCHERICHIA COLI Escherichia coli - metabolism Escherichia coli Proteins EXPERIMENTACION IN VIVO EXPERIMENTATION IN VIVO Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial - physiology Genetic engineering Genetic technics Heat-Shock Proteins - biosynthesis HSP40 Heat-Shock Proteins IN VIVO EXPERIMENTATION Methods. Procedures. Technologies Modification of gene expression level Molecular Chaperones - biosynthesis PAGRUS Pagrus major Perciformes - metabolism Plasmids - genetics Recombinant Proteins - biosynthesis Solubility Temperature TEXTURA TEXTURE transglutaminase Transglutaminases - metabolism |
| title | Overproduction of dnaJ in Escherichia coli improves in vivo solubility of the recombinant fish-derived transglutaminase |
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