期刊
FEMS MICROBIOLOGY LETTERS
卷 311, 期 2, 页码 133-139出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2010.02081.x
关键词
extended signal peptide region (ESPR); Escherichia coli; autotransporter; plasmid-encoded toxin (Pet); secretion
类别
资金
- University of Birmingham Medical School
- CNPq, Brazil
- BBSRC
- Medical Research Council [G0900857] Funding Source: researchfish
- MRC [G0900857] Funding Source: UKRI
The plasmid-encoded toxin, Pet, a prototypical member of the serine protease autotransporters of the Enterobacteriaceae, possesses an unusually long signal peptide, which can be divided into five regions termed N1 (charged), H1 (hydrophobic), N2, H2 and C (cleavage site) domains. The N1 and H1 regions correspond to a conserved N-terminal extension previously designated the extended signal peptide region (ESPR), while the N2, H2 and C regions resemble typical Sec-dependent signal sequences and exhibit considerable sequence variability. We have shown previously that the ESPR directs Sec-dependent, post-translational translocation of Pet across the bacterial inner membrane. In this study, we demonstrate that the ESPR is not essential for the secretion or the function of Pet.
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