The unusual extended signal peptide region is not required for secretion and function of an Escherichia coli autotransporter

Denisse L Leyton, Maria das Gracas de Luna, Yanina R Sevastsyanovich, Karina T Jensen, Douglas F Browning, Anthony Scott-Tucker, Ian R Henderson

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)133 - 139
Number of pages7
JournalFEMS Microbiology Letters
Volume311
Issue number2
DOIs
Publication statusPublished - 2010
Externally publishedYes

Cite this