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Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology
Protein Secretion, Page 1 of 2
< Previous page | Next page > /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap49-1.gif /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap49-2.gifAbstract:
The basic mechanism by which proteins are transported across membranes appears to be universal, with important features conserved between bacteria and eukaryotes. Protein secretion across the Bacillus subtilis cell envelope is a complex process. Protein transport involves an interaction between the exported protein and the cellular secretion factors. Some of the characteristics of protein secretion in Escherichia coli and B. subtilis are similar. The first part of this chapter discusses some of the structural features of the B. subtilis exoproteins and their role in protein secretion. This discussion is followed by an outline of the approaches taken to define the components of B. subtilis secretion machinery and of one's current knowledge of protein secretion in B. subtilis. In this discussion, the term “translocation” refers to the transfer of protein across the membrane. The signal sequence mutants described were constructed to improve the secretion efficiency of the wheat α-amylase signal sequence in B. subtilis. The wheat α--amylase signal peptide can transport LVS and E. coli alkaline phosphatase from B. subtilis, but the kinetics of transport were slower than those observed with Bacillus signal peptides. This observation underlines an important role played by the mature sequence in protein secretion. The difference in phenotype between E. coli and B. subtilis was useful in cloning the B. subtilis leader peptidase gene. These two complementary approaches have identified mutations within the same structural genes, underlining the importance of these genes in protein export.
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Signal peptide sequences a
Signal peptide sequences a
Lipoprotein signal sequences a
Lipoprotein signal sequences a