The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease
1 Department of Molecular Microbiology, Institute of Molecular Cell Biology, VU University, 1081 HV Amsterdam, The Netherlands 2 Center for Biomembrane Research, Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, SE-106 91 Stockholm, Sweden 3 Department of Molec...
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Published in: | Microbiology (Society for General Microbiology) 2009-12, Vol.155 (12), p.3982-3991 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | eng |
Subjects: | |
Online Access: | Get full text |
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Summary: | 1 Department of Molecular Microbiology, Institute of Molecular Cell Biology, VU University, 1081 HV Amsterdam, The Netherlands
2 Center for Biomembrane Research, Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, SE-106 91 Stockholm, Sweden
3 Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, VU University, 1081 HV Amsterdam, The Netherlands
Autotransporters are large virulence factors secreted by Gram-negative bacteria. They are synthesized with a C-terminal domain that forms a β -barrel pore in the outer membrane implicated in translocation of the upstream passenger domain across the outer membrane. However, recent structural data suggest that the diameter of the β -barrel pore is not sufficient to allow the passage of partly folded structures observed for several autotransporters. Here, we have used a stalled translocation intermediate of the autotransporter Hbp to identify components involved in insertion and translocation of the protein across the outer membrane. At this intermediate stage the β -domain was not inserted and folded as an integral β -barrel in the outer membrane whereas part of the passenger was surface exposed. The intermediate was copurified with the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex that catalyse the insertion and assembly of outer-membrane proteins. The data suggest a critical role for this general machinery in the translocation of autotransporters across the outer membrane.
Correspondence Joen Luirink joen.luirink{at}falw.vu.nl
Abbreviations: AT, autotransporter; DSP, dithiobis(succinimidylpropionate); DSS, disuccinimidyl suberate; OM, outer membrane; OMP, outer-membrane protein
Four supplementary figures and a supplementary table are available with the online version of this paper. |
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ISSN: | 1350-0872 1465-2080 1465-2080 |