期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 5, 页码 506-U63出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2261
关键词
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资金
- National Health & Medical Research Council (NHMRC) of Australia [508911]
- NHMRC [606788]
- ARC
- BBSRC
- BBSRC [BB/G00773X/1] Funding Source: UKRI
- MRC [G0700151, G0801209] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G00773X/1] Funding Source: researchfish
- Medical Research Council [G0700151, G0801209] Funding Source: researchfish
Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called 'autotransporters' have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by bacterial pathogens.
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