Chauhan, N., Hatlem, D., Orwick-Rydmark, M., Schneider, K., Floetenmeyer, M., Van Rossum, B., Leo, J.C. ORCID: 0000-0002-7066-7527 and Linke, D., 2019. Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA). Molecular Microbiology, 111 (3), pp. 844-862. ISSN 0950-382X
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Abstract
Trimeric autotransporter adhesins (TAAs) are a subset of a larger protein family called the type V secretion systems. They are localized on the cell surface of Gram‐negative bacteria, function as mediators of attachment to inorganic surfaces and host cells, and thus include important virulence factors. Yersinia adhesin A (YadA) from Yersinia enterocolitica is a prototypical TAA that is used extensively to study the structure and function of the type Vc secretion system. A solid‐state NMR study of the membrane anchor domain of YadA previously revealed a flexible stretch of small residues, termed the ASSA region, that links the membrane anchor to the stalk domain. In this study, we present evidence that single amino acid proline substitutions produce two different conformers of the membrane anchor domain of YadA; one with the N‐termini facing the extracellular surface, and a second with the N‐termini located in the periplasm. We propose that TAAs adopt a hairpin intermediate during secretion, as has been shown before for other subtypes of the type V secretion system. As the YadA transition state intermediate can be isolated from the outer membrane, future structural studies should be possible to further unravel details of the autotransport process.
Item Type: | Journal article | ||||
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Publication Title: | Molecular Microbiology | ||||
Creators: | Chauhan, N., Hatlem, D., Orwick-Rydmark, M., Schneider, K., Floetenmeyer, M., Van Rossum, B., Leo, J.C. and Linke, D. | ||||
Publisher: | Wiley-Blackwell | ||||
Date: | March 2019 | ||||
Volume: | 111 | ||||
Number: | 3 | ||||
ISSN: | 0950-382X | ||||
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Divisions: | Schools > School of Science and Technology | ||||
Record created by: | Linda Sullivan | ||||
Date Added: | 25 Sep 2019 13:33 | ||||
Last Modified: | 13 Feb 2020 03:00 | ||||
URI: | https://irep.ntu.ac.uk/id/eprint/37775 |
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