The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate

Oberhettinger, P., Leo, J.C. ORCID: 0000-0002-7066-7527, Linke, D., Autenrieth, I.B. and Schütz, M.S., 2015. The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate. Journal of Biological Chemistry, 290 (3), pp. 1837-1849. ISSN 1083-351X

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Abstract

Autotransporter proteins comprise a large family of virulence factors that consist of a-barrel translocation unit and an extracellular effector or passenger domain. The -barrel anchors the protein to the outer membrane of Gram-negative bacteria and facilitates the transport of the passenger domain onto the cell surface. By inserting an epitope tag into the N terminus of the passenger domain of the inverse autotransporter intimin, we generated a mutant defective in autotransport. Using this stalled mutant, we could show that (i) at the time point of stalling, the -barrel appears folded; (ii) the stalled autotransporter is associated with BamA and SurA; (iii) the stalled intimin is decorated with large amounts of SurA; (iv) the stalled autotransporter is not degraded by periplasmic proteases; and (v) inverse autotransporter passenger domains are translocated by a hairpin mechanism. Our results suggest a function for the BAM complex not only in insertion and folding of the -barrel but also for passenger translocation.

Item Type: Journal article
Publication Title: Journal of Biological Chemistry
Creators: Oberhettinger, P., Leo, J.C., Linke, D., Autenrieth, I.B. and Schütz, M.S.
Publisher: American Society for Biochemistry and Molecular Biology (ASBMB)
Date: 16 January 2015
Volume: 290
Number: 3
ISSN: 1083-351X
Identifiers:
NumberType
10.1074/jbc.m114.604769DOI
Rights: © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Divisions: Schools > School of Science and Technology
Depositing User: Jill Tomkinson
Date Added: 18 Jun 2019 13:40
Last Modified: 25 Jun 2019 13:05
URI: http://irep.ntu.ac.uk/id/eprint/36842

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