Autoprocessing of the Escherichia coli AIDA-I Autotransporter
نویسندگان
چکیده
منابع مشابه
Autoprocessing of the Escherichia coli AIDA-I autotransporter: a new mechanism involving acidic residues in the junction region.
The cleavage of the autotransporter adhesin involved in diffuse adherence (AIDA-I) of Escherichia coli yields a membrane-embedded fragment, AIDAc, and an extracellular fragment, the mature AIDA-I adhesin. The latter remains noncovalently associated with AIDAc but can be released by heat treatment. In this study we determined the mechanism of AIDA-I cleavage. We showed that AIDA-I processing is ...
متن کاملPresentation of functional organophosphorus hydrolase fusions on the surface of Escherichia coli by the AIDA-I autotransporter pathway.
We report, the surface presentation of organophosphorus hydrolase (OPH) and green fluorescent protein (GFP) fusions by employing the adhesin-involved-in-diffuse-adherence (AIDA-I) translocator domain as a transporter and anchoring motif. The surface location of the OPH-GFP fusion protein was confirmed by immunofluorescence microscopy, and protease accessibility, followed by Western blotting ana...
متن کاملAutodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter.
Members of the protein family of immunoglobulin A1 protease-like autotransporters comprise multidomain precursors consisting of a C-terminal autotransporter domain that promotes the translocation of N-terminally attached passenger domains across the cell envelopes of gram-negative bacteria. Several autotransporter domains have recently been shown to efficiently promote the export of heterologou...
متن کاملProteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I).
The Escherichia coli adhesin involved in diffuse adherence (AIDA-I), like many other autotransporter proteins, is released in the periplasm as a proprotein undergoing proteolytic processing after its translocation across the outer membrane. The proprotein is cleaved into a membrane-embedded fragment, AIDAc, and an extracellular fragment, the mature AIDA-I adhesin. The latter remains noncovalent...
متن کاملCharacterization of the essential transport function of the AIDA-I autotransporter and evidence supporting structural predictions.
The current model for autodisplay suggests a mechanism that allows a passenger protein to be translocated across the outer membrane by coordinate action of a C-terminal beta-barrel and its preceding linking region. The passenger protein, linker, and beta-barrel are together termed the autotransporter, while the linker and beta-barrel are here referred to as the translocation unit (TU). We chara...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2009
ISSN: 0021-9258
DOI: 10.1074/jbc.m109.010108