Literature DB >> 26859957

[Structural and Functional Organization of the Signal Peptide of ProEnterotoxin B from Staphylococcus aureus].

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

Abstract

A series of genes of proenterotoxin 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 proprotein 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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Year:  2015        PMID: 26859957

Source DB:  PubMed          Journal:  Prikl Biokhim Mikrobiol        ISSN: 0555-1099


  2 in total

1.  Expression and function of an Hac1-regulated multi-copy xylanase gene in Saccharomyces cerevisiae.

Authors:  Changjie Bao; Jiping Li; Huan Chen; Yang Sun; Gang Wang; Guang Chen; Sitong Zhang
Journal:  Sci Rep       Date:  2020-07-15       Impact factor: 4.379

Review 2.  Increasing the Efficiency of the Accumulation of Recombinant Proteins in Plant Cells: The Role of Transport Signal Peptides.

Authors:  Sergey M Rozov; Elena V Deineko
Journal:  Plants (Basel)       Date:  2022-09-28
  2 in total

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