A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism
| Autor: | Damon Huber, Lisa M. Cooper, Ian R. Henderson, Anthony Scott-Tucker, Sue M. Turner, Mickaël Desvaux, James P. Nataro |
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| Přispěvatelé: | Unité de Microbiologie (MIC), Institut National de la Recherche Agronomique (INRA), University of Birmingham, Department of Microbiology and Molecular Genetics, Harvard Medical School [Boston] (HMS), University of Maryland School of Medicine, University of Maryland System |
| Rok vydání: | 2006 |
| Předmět: |
Signal peptide
INNER MEMBRANE TRANSLOCATION 2-PARTNER SECRETION Molecular Sequence Data RECOGNITION PARTICLE BACTERIAL PATHOGENESIS VIRULENCE FACTOR Biology Microbiology PATHWAY Cell membrane 03 medical and health sciences Bacterial Proteins Enterobacteriaceae AUTOTRANSPORTER PROTEINS medicine Inner membrane Secretion Amino Acid Sequence GRAM-NEGATIVE BACTERIA Peptide sequence 030304 developmental biology 0303 health sciences MEMBRANE-PROTEINS SIGNAL PEPTIDE 030306 microbiology Cell Membrane Serine Endopeptidases ESCHERICHIA-COLI PERIPLASM SUBSET EXPORT Cell biology Transport protein Protein Structure Tertiary AUTOTRANSPORTER Protein Transport DEPENDENT TRANSLOCATION [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Secretory protein medicine.anatomical_structure Biochemistry Membrane protein TYPE V PROTEIN SECRETION SYSTEM Protein Biosynthesis |
| Zdroj: | Microbiology Microbiology, Microbiology Society, 2007, 153 (1), pp.59-70. ⟨10.1099/mic.0.29091-0⟩ |
| ISSN: | 1350-0872 1465-2080 |
| DOI: | 10.1099/mic.0.29091-0⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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