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Structural and functional organization of the signal peptide of pro-enterotoxin B from Staphylococcus aureus

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Abstract

A series of genes of pro-enterotoxin B from Staphylococcus aureus containing signal peptide mutant forms was constructed in order to study the functional roles of the introduced mutations. It was shown that a continuous mutation in the n-region of the signal peptide does not affect the secretion efficiency of proenterotoxin B, in contrast to the analogous mutation in the h-region. Point mutations of the pro-protein signal peptide, including the N-terminal amino acid residue of the mature protein, were obtained. It was shown that the introduced structural changes cause a decrease in secretion efficiency and a redistribution of the protein in various compartments of Escherichia coli cells.

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Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia

    N. N. Mordkovich, N. A. Okorokova & V. P. Veiko

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  1. N. N. Mordkovich
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  2. N. A. Okorokova
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  3. V. P. Veiko
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Correspondence to V. P. Veiko.

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Original Russian Text © N.N. Mordkovich, N.A. Okorokova, V.P. Veiko, 2015, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2015, Vol. 51, No. 6, pp. 561–569.

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Mordkovich, N.N., Okorokova, N.A. & Veiko, V.P. Structural and functional organization of the signal peptide of pro-enterotoxin B from Staphylococcus aureus . Appl Biochem Microbiol 51, 641–648 (2015). https://doi.org/10.1134/S0003683815060101

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