期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 3, 页码 1837-1849出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.604769
关键词
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资金
- German Research Council (DFG) [SFB 766]
- FEMS
- Fortune program [F1433253]
- TUFF of the University Clinics Tubingen [E05003231]
- German Center for Infection Research (DZIF)
Autotransporter proteins comprise a large family of virulence factors that consist of a beta-barrel translocation unit and an extracellular effector or passenger domain. The beta-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 beta-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 beta-barrel but also for passenger translocation.
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