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Volume 153, Issue 1

A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism Free

Abstract

Members of the type V secretion family are among the most prevalent secreted proteins in Gram-negative bacteria. A subset of this family, including Pet, the prototypical member of the serine proteases, possess unusual signal peptides which can be divided into five regions termed N1 (charged), H1 (hydrophobic), N2, H2 and C (cleavage site) domains. The N1 and H1 regions, which the authors have named the extended signal peptide region (ESPR), demonstrate remarkable conservation. In contrast, the N2, H2 and C regions show significant variability, and are reminiscent of typical Sec-dependent signal sequences. Despite several investigations, the function of the ESPR remains obscure. Here, it is shown that proteins possessing the ESPR are translocated in a posttranslational fashion. The presence of the ESPR severely impairs inner membrane translocation. Mutational analysis suggests that the ESPR delays inner membrane translocation by adopting a particular conformation, or by interacting with a cytoplasmic or inner membrane co-factor, prior to inner membrane translocation.

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Keyword(s): EP-PCR, error-prone PCR , ESPR, extended signal peptide region , FHA, filamentous haemagglutinin , SPATE, serine protease autotransporter of the Enterobacteriaceae , SRP, signal recognition particle , T5SS, type V secretion system , TU, translocation unit and XP, 5-bromo-4-chloro-3-indolyl phosphate
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2007-01-01
2024-04-19
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A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism
Microbiology 153, 59 (2007); https://doi.org/10.1099/mic.0.29091-0
/content/journal/micro/10.1099/mic.0.29091-0
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