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• W1535133733 abstract "Research Article1 October 1984free access Secretion cloning vectors in Escherichia coli. J. Ghrayeb J. Ghrayeb Search for more papers by this author H. Kimura H. Kimura Search for more papers by this author M. Takahara M. Takahara Search for more papers by this author H. Hsiung H. Hsiung Search for more papers by this author Y. Masui Y. Masui Search for more papers by this author M. Inouye M. Inouye Search for more papers by this author J. Ghrayeb J. Ghrayeb Search for more papers by this author H. Kimura H. Kimura Search for more papers by this author M. Takahara M. Takahara Search for more papers by this author H. Hsiung H. Hsiung Search for more papers by this author Y. Masui Y. Masui Search for more papers by this author M. Inouye M. Inouye Search for more papers by this author Author Information J. Ghrayeb, H. Kimura, M. Takahara, H. Hsiung, Y. Masui and M. Inouye The EMBO Journal (1984)3:2437-2442https://doi.org/10.1002/j.1460-2075.1984.tb02151.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The DNA fragment coding for the signal peptide of the OmpA protein, a major outer membrane protein of Escherichia coli, has been inserted into the high-level expression vectors, pIN-III. A foreign DNA fragment can be cloned in any one of the three reading frames at the unique EcoRI, HindIII or BamHI sites immediately after the ompA signal peptide coding sequence. The cloned foreign gene is under the control of both the lpp promoter and the lac promoter-operator. The expression of the gene is regulated by the lac repressor produced by the same vectors. Using the pIN-III-ompA vector, the DNA fragment coding for only the mature portion of beta-lactamase was inserted into the EcoRI site. Upon induction of gene expression, beta-lactamase was secreted into the periplasmic space. The ompA signal peptide was correctly removed resulting in the production of beta-lactamase with four extra amino acid residues (Gly-Ile-Pro-Gly) at its amino terminus due to the linker sequence in the vector. After a 3-h induction, beta-lactamase was accumulated to 20% of total cellular protein without any detectable accumulation of pro-beta-lactamase. Using oligonucleotide-directed site-specific mutagenesis, we have also removed the linker sequence and upon induction of gene expression, beta-lactamase with the authentic NH2-terminal sequence was produced, in even larger amounts than the beta-lactamase with the linker sequence. Next ArticlePrevious Article Volume 3Issue 101 October 1984In this issue RelatedDetailsLoading ..." @default.
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• W1535133733 title "Secretion cloning vectors in Escherichia coli." @default.
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• W1535133733 doi "https://doi.org/10.1002/j.1460-2075.1984.tb02151.x" @default.
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