TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion
The twin-arginine translocation (Tat) pathway in Corynebacterium glutamicum has been described previously. The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We pr...
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| Veröffentlicht in: | Applied and Environmental Microbiology 2009-02, Vol.75 (3), p.603-607 |
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| creator | Kikuchi, Yoshimi Itaya, Hiroshi Date, Masayo Matsui, Kazuhiko Wu, Long-Fei |
| description | The twin-arginine translocation (Tat) pathway in Corynebacterium glutamicum has been described previously. The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We previously demonstrated that Chryseobacterium proteolyticum pro-protein glutaminase (pro-PG) and Streptomyces mobaraensis pro-transglutaminase (pro-TG) could be secreted via the Tat pathway in C. glutamicum. Here we report that the amounts of pro-PG secreted were more than threefold larger when TatC or TatAC was overexpressed, and there was a further threefold increase when TatABC was overexpressed. These results show that the amount of TatC protein is the first bottleneck and the amount of TatB protein is the second bottleneck in Tat-dependent protein secretion in C. glutamicum. In addition, the amount of pro-TG that accumulated via the Tat pathway when TatABC was overexpressed with the TorA signal peptide in C. glutamicum was larger than the amount that accumulated via the Sec pathway. We concluded that TatABC overexpression improves Tat-dependent pro-PG and pro-TG secretion in C. glutamicum. |
| doi_str_mv | 10.1128/AEM.01874-08 |
| format | Article |
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The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We previously demonstrated that Chryseobacterium proteolyticum pro-protein glutaminase (pro-PG) and Streptomyces mobaraensis pro-transglutaminase (pro-TG) could be secreted via the Tat pathway in C. glutamicum. Here we report that the amounts of pro-PG secreted were more than threefold larger when TatC or TatAC was overexpressed, and there was a further threefold increase when TatABC was overexpressed. These results show that the amount of TatC protein is the first bottleneck and the amount of TatB protein is the second bottleneck in Tat-dependent protein secretion in C. glutamicum. In addition, the amount of pro-TG that accumulated via the Tat pathway when TatABC was overexpressed with the TorA signal peptide in C. glutamicum was larger than the amount that accumulated via the Sec pathway. We concluded that TatABC overexpression improves Tat-dependent pro-PG and pro-TG secretion in C. glutamicum.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>EISSN: 1098-6596</identifier><identifier>DOI: 10.1128/AEM.01874-08</identifier><identifier>PMID: 19074606</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amidohydrolases - genetics ; Amidohydrolases - metabolism ; Amino acids ; Bacteria ; Bacterial Proteins - metabolism ; Bacteriology ; Biochemistry ; Biological and medical sciences ; Chryseobacterium - enzymology ; Chryseobacterium - genetics ; Chryseobacterium proteolyticum ; Corynebacterium glutamicum - genetics ; Corynebacterium glutamicum - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Dosage ; Gene Expression ; Glutaminase ; Membrane Transport Proteins - metabolism ; Microbiology ; Physiology and Biotechnology ; Proteins ; Recombinant Proteins - metabolism ; Streptomyces - enzymology ; Streptomyces - genetics ; Transglutaminases - genetics ; Transglutaminases - metabolism</subject><ispartof>Applied and Environmental Microbiology, 2009-02, Vol.75 (3), p.603-607</ispartof><rights>2009 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Feb 2009</rights><rights>Copyright © 2009, American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-492e4e25a59adfeb9186d33ffa796eae54fec02f23a4c060209f5eb89d7567e83</citedby><cites>FETCH-LOGICAL-c519t-492e4e25a59adfeb9186d33ffa796eae54fec02f23a4c060209f5eb89d7567e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2632119/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2632119/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,3176,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21140926$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19074606$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kikuchi, Yoshimi</creatorcontrib><creatorcontrib>Itaya, Hiroshi</creatorcontrib><creatorcontrib>Date, Masayo</creatorcontrib><creatorcontrib>Matsui, Kazuhiko</creatorcontrib><creatorcontrib>Wu, Long-Fei</creatorcontrib><title>TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>The twin-arginine translocation (Tat) pathway in Corynebacterium glutamicum has been described previously. The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We previously demonstrated that Chryseobacterium proteolyticum pro-protein glutaminase (pro-PG) and Streptomyces mobaraensis pro-transglutaminase (pro-TG) could be secreted via the Tat pathway in C. glutamicum. Here we report that the amounts of pro-PG secreted were more than threefold larger when TatC or TatAC was overexpressed, and there was a further threefold increase when TatABC was overexpressed. These results show that the amount of TatC protein is the first bottleneck and the amount of TatB protein is the second bottleneck in Tat-dependent protein secretion in C. glutamicum. In addition, the amount of pro-TG that accumulated via the Tat pathway when TatABC was overexpressed with the TorA signal peptide in C. glutamicum was larger than the amount that accumulated via the Sec pathway. We concluded that TatABC overexpression improves Tat-dependent pro-PG and pro-TG secretion in C. glutamicum.</description><subject>Amidohydrolases - genetics</subject><subject>Amidohydrolases - metabolism</subject><subject>Amino acids</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chryseobacterium - enzymology</subject><subject>Chryseobacterium - genetics</subject><subject>Chryseobacterium proteolyticum</subject><subject>Corynebacterium glutamicum - genetics</subject><subject>Corynebacterium glutamicum - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Dosage</subject><subject>Gene Expression</subject><subject>Glutaminase</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Microbiology</subject><subject>Physiology and Biotechnology</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces - genetics</subject><subject>Transglutaminases - genetics</subject><subject>Transglutaminases - metabolism</subject><issn>0099-2240</issn><issn>1098-5336</issn><issn>1098-6596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v0zAYhyMEYmVw4wwREpzIeP0Z-4JUyoBJQ0PaduBkue6b1lMSFzsp7L_HodX4uHCyJT9-_Hv9K4qnBE4IoerN_PTzCRBV8wrUvWJGQKtKMCbvFzMArStKORwVj1K6AQAOUj0sjoiGmkuQs-LrlR3m7xblxQ4j_thGTMmHvjzrtjHsMJWLEG97XFo3YPRjV67bcbCdd3mbb1bvcYv9Cvuh_BLDgL4vL9FFHLLjcfGgsW3CJ4f1uLj-cHq1-FSdX3w8W8zPKyeIHiquKXKkwgptVw0uNVFyxVjT2FpLtCh4gw5oQ5nlDiRQ0I3ApdKrWsgaFTsu3u6923HZ4crlMNG2Zht9Z-OtCdabv096vzHrsDNUMkqIzoJXB0EM30ZMg-l8cti2tscwJiOl4rrm8F-QEq4l01OkF_-AN2GMff4FQ0FoybWann29h1wMKUVs7iITMFOzJjdrfjVrYHI--3PM3_Chygy8PAA2Ods20fbOpzsuj8pB04kr99zGrzfffURjU2csdqYWhhkJLCPP90hjg7HrmDXXlxQIAyKUoIyyn2yFwM8</recordid><startdate>20090201</startdate><enddate>20090201</enddate><creator>Kikuchi, Yoshimi</creator><creator>Itaya, Hiroshi</creator><creator>Date, Masayo</creator><creator>Matsui, Kazuhiko</creator><creator>Wu, Long-Fei</creator><general>American Society for Microbiology</general><general>American Society for Microbiology (ASM)</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>7QL</scope><scope>7QO</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090201</creationdate><title>TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion</title><author>Kikuchi, Yoshimi ; Itaya, Hiroshi ; Date, Masayo ; Matsui, Kazuhiko ; Wu, Long-Fei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-492e4e25a59adfeb9186d33ffa796eae54fec02f23a4c060209f5eb89d7567e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amidohydrolases - genetics</topic><topic>Amidohydrolases - metabolism</topic><topic>Amino acids</topic><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chryseobacterium - enzymology</topic><topic>Chryseobacterium - genetics</topic><topic>Chryseobacterium proteolyticum</topic><topic>Corynebacterium glutamicum - genetics</topic><topic>Corynebacterium glutamicum - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Dosage</topic><topic>Gene Expression</topic><topic>Glutaminase</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Microbiology</topic><topic>Physiology and Biotechnology</topic><topic>Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces - genetics</topic><topic>Transglutaminases - genetics</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kikuchi, Yoshimi</creatorcontrib><creatorcontrib>Itaya, Hiroshi</creatorcontrib><creatorcontrib>Date, Masayo</creatorcontrib><creatorcontrib>Matsui, Kazuhiko</creatorcontrib><creatorcontrib>Wu, Long-Fei</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kikuchi, Yoshimi</au><au>Itaya, Hiroshi</au><au>Date, Masayo</au><au>Matsui, Kazuhiko</au><au>Wu, Long-Fei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2009-02-01</date><risdate>2009</risdate><volume>75</volume><issue>3</issue><spage>603</spage><epage>607</epage><pages>603-607</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><eissn>1098-6596</eissn><coden>AEMIDF</coden><abstract>The twin-arginine translocation (Tat) pathway in Corynebacterium glutamicum has been described previously. The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We previously demonstrated that Chryseobacterium proteolyticum pro-protein glutaminase (pro-PG) and Streptomyces mobaraensis pro-transglutaminase (pro-TG) could be secreted via the Tat pathway in C. glutamicum. Here we report that the amounts of pro-PG secreted were more than threefold larger when TatC or TatAC was overexpressed, and there was a further threefold increase when TatABC was overexpressed. These results show that the amount of TatC protein is the first bottleneck and the amount of TatB protein is the second bottleneck in Tat-dependent protein secretion in C. glutamicum. In addition, the amount of pro-TG that accumulated via the Tat pathway when TatABC was overexpressed with the TorA signal peptide in C. glutamicum was larger than the amount that accumulated via the Sec pathway. We concluded that TatABC overexpression improves Tat-dependent pro-PG and pro-TG secretion in C. glutamicum.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>19074606</pmid><doi>10.1128/AEM.01874-08</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amidohydrolases - genetics Amidohydrolases - metabolism Amino acids Bacteria Bacterial Proteins - metabolism Bacteriology Biochemistry Biological and medical sciences Chryseobacterium - enzymology Chryseobacterium - genetics Chryseobacterium proteolyticum Corynebacterium glutamicum - genetics Corynebacterium glutamicum - metabolism Fundamental and applied biological sciences. Psychology Gene Dosage Gene Expression Glutaminase Membrane Transport Proteins - metabolism Microbiology Physiology and Biotechnology Proteins Recombinant Proteins - metabolism Streptomyces - enzymology Streptomyces - genetics Transglutaminases - genetics Transglutaminases - metabolism |
| title | TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion |
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