Herfurth, M., Treuner-Lange, A., Glatter, T. et al. (4 more authors) (2022) A noncanonical cytochrome c stimulates calcium binding by PilY1 for type IVa pili formation. Proceedings of the National Academy of Sciences, 119 (6). e2115061119. ISSN 0027-8424
Abstract
Type IVa pili (T4aP) are versatile bacterial cell surface structures that undergo extension/adhesion/retraction cycles powered by the cell envelope–spanning T4aP machine. In this machine, a complex composed of four minor pilins and PilY1 primes T4aP extension and is also present at the pilus tip mediating adhesion. Similar to many several other bacteria, Myxococcus xanthus contains multiple minor pilins/PilY1 sets that are incompletely understood. Here, we report that minor pilins and PilY1 (PilY1.1) of cluster_1 form priming and tip complexes contingent on calcium and a noncanonical cytochrome c (TfcP) with an unusual His/Cys heme ligation. We provide evidence that TfcP is unlikely to participate in electron transport and instead stimulates calcium binding by PilY1.1 at low-calcium concentrations, thereby stabilizing PilY1.1 and enabling T4aP function in a broader range of calcium concentrations. These results not only identify a previously undescribed function of cytochromes c but also illustrate how incorporation of an accessory factor expands the environmental range under which the T4aP system functions.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2022 The Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY) https://creativecommons.org/licenses/by/4.0/. |
Keywords: | type IV pili; cytochrome c; PilY1; bacterial adhesin; minor pilin |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 18 Feb 2022 08:19 |
Last Modified: | 10 Feb 2023 14:12 |
Status: | Published |
Publisher: | National Academy of Sciences of the United States of America |
Refereed: | Yes |
Identification Number: | 10.1073/pnas.2115061119 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:183762 |