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

Tools

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

Preview

Text
14081_Leo.pdf - Published version
Download (3MB) | Preview

Official URL: http://doi.org/10.1074/jbc.m114.604769

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