Journal
MICROBIOLOGY-SGM
Volume 153, Issue -, Pages 59-70Publisher
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.29091-0
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Funding
- MRC [G0700151] Funding Source: UKRI
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI043617] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM041883] Funding Source: NIH RePORTER
- Medical Research Council [G0700151] Funding Source: Medline
- NIAID NIH HHS [AI43617] Funding Source: Medline
- NIGMS NIH HHS [GM41883] Funding Source: Medline
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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 Enterobacteriaceae 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 ESPIR 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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