{"title":"单根希瓦氏菌MR-1细菌细胞中异源基因表达蛋白易位系统的研究","authors":"N N Mordkovich, N A Okorokova, V P Veiko","doi":"10.7868/s0555109915030125","DOIUrl":null,"url":null,"abstract":"<p><p>A comparison of the primary structures of the protein translocation Sec-system proteins in the Shewanella oneidensis MR-1 and Escherichia coli bacteria was carried out. The process of translocation of recombinant pro-enteroxins (SEB and SEH) from Staphylococcus aureus and pro-streptavidin (SAV) from Streptomyces avidinii in the S. oneidensis MR-1 and E. coli cell periplasm was studied. It was demonstrated that these marker proteins are transferred into the periplasmic space of the S. oneidensis MR-1 transformant strain cells. The identity of N-terminal amino acid sequences of mature recombinant SEB, SEH, and SAV proteins (generated during post-translation proteolysis of leader peptide by the Sec-system both in E. coli and S. oneidensis MR-1) was established.</p>","PeriodicalId":20415,"journal":{"name":"Prikladnaia biokhimiia i mikrobiologiia","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2015-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Investigation of Protein Translocation Sec-System with Heterologous Gene Expression in Shewanella oneidensis MR-1 Bacterium Cells].\",\"authors\":\"N N Mordkovich, N A Okorokova, V P Veiko\",\"doi\":\"10.7868/s0555109915030125\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A comparison of the primary structures of the protein translocation Sec-system proteins in the Shewanella oneidensis MR-1 and Escherichia coli bacteria was carried out. The process of translocation of recombinant pro-enteroxins (SEB and SEH) from Staphylococcus aureus and pro-streptavidin (SAV) from Streptomyces avidinii in the S. oneidensis MR-1 and E. coli cell periplasm was studied. It was demonstrated that these marker proteins are transferred into the periplasmic space of the S. oneidensis MR-1 transformant strain cells. The identity of N-terminal amino acid sequences of mature recombinant SEB, SEH, and SAV proteins (generated during post-translation proteolysis of leader peptide by the Sec-system both in E. coli and S. oneidensis MR-1) was established.</p>\",\"PeriodicalId\":20415,\"journal\":{\"name\":\"Prikladnaia biokhimiia i mikrobiologiia\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2015-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Prikladnaia biokhimiia i mikrobiologiia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.7868/s0555109915030125\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Prikladnaia biokhimiia i mikrobiologiia","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.7868/s0555109915030125","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Investigation of Protein Translocation Sec-System with Heterologous Gene Expression in Shewanella oneidensis MR-1 Bacterium Cells].
A comparison of the primary structures of the protein translocation Sec-system proteins in the Shewanella oneidensis MR-1 and Escherichia coli bacteria was carried out. The process of translocation of recombinant pro-enteroxins (SEB and SEH) from Staphylococcus aureus and pro-streptavidin (SAV) from Streptomyces avidinii in the S. oneidensis MR-1 and E. coli cell periplasm was studied. It was demonstrated that these marker proteins are transferred into the periplasmic space of the S. oneidensis MR-1 transformant strain cells. The identity of N-terminal amino acid sequences of mature recombinant SEB, SEH, and SAV proteins (generated during post-translation proteolysis of leader peptide by the Sec-system both in E. coli and S. oneidensis MR-1) was established.