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PilT and PilU are homohexameric ATPases that coordinate to retract type IVa pili

Jennifer L. Chlebek, Hannah Q. Hughes, Aleksandra S. Ratkiewicz, Rasman Rayyan, Joseph Che-Yen Wang, Brittany E. Herrin, Triana N. Dalia, Nicolas Biais, View ORCID ProfileAnkur B. Dalia
doi: https://doi.org/10.1101/634048
Jennifer L. Chlebek
1Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405.
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Hannah Q. Hughes
1Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405.
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Aleksandra S. Ratkiewicz
2Biology Department, CUNY Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210 and Graduate Center of CUNY, 365 5th Avenue, NY 10016.
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Rasman Rayyan
2Biology Department, CUNY Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210 and Graduate Center of CUNY, 365 5th Avenue, NY 10016.
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Joseph Che-Yen Wang
3Electron Microscopy Center, Indiana University, Bloomington, IN 47405.
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Brittany E. Herrin
1Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405.
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Triana N. Dalia
1Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405.
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Nicolas Biais
2Biology Department, CUNY Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210 and Graduate Center of CUNY, 365 5th Avenue, NY 10016.
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Ankur B. Dalia
1Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405.
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  • ORCID record for Ankur B. Dalia
  • For correspondence: ankdalia@indiana.edu
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Abstract

Bacterial type IV pili are critical for diverse biological processes including horizontal gene transfer, surface sensing, biofilm formation, adherence, motility, and virulence. These dynamic appendages extend and retract from the cell surface. In many type IVa pilus systems, extension occurs through the action of an extension ATPase, often called PilB, while optimal retraction requires the action of a retraction ATPase, PilT. Many type IVa systems also encode a homolog of PilT called PilU. However, the function of this protein has remained unclear because pilU mutants exhibit inconsistent phenotypes among type IV pilus systems and because it is relatively understudied compared to PilT. Here, we study the type IVa competence pilus of Vibrio cholerae as a model system to define the role of PilU. We show that the ATPase activity of PilU is critical for pilus retraction in PilT Walker A and/or Walker B mutants. PilU does not, however, contribute to pilus retraction in ΔpilT strains. Thus, these data suggest that PilU is a bona fide retraction ATPase that supports pilus retraction in a PilT-dependent manner. We also found that a ΔpilU mutant exhibited a reduction in the force of retraction suggesting that PilU is important for generating maximal retraction forces. Additional in vitro and in vivo data show that PilT and PilU act as independent homo-hexamers that may form a complex to facilitate pilus retraction. Finally, we demonstrate that the role of PilU as a PilT-dependent retraction ATPase is conserved in Acinetobacter baylyi, suggesting that the role of PilU described here may be broadly applicable to other type IVa pilus systems.

Author Summary Almost all bacterial species use thin surface appendages called pili to interact with their environments. These structures are critical for the virulence of many pathogens and represent one major way that bacteria share DNA with one another, which contributes to the spread of antibiotic resistance. To carry out their function, pili dynamically extend and retract from the bacterial surface. Here, we show that retraction of pili in some systems is determined by the combined activity of two motor ATPase proteins.

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Posted September 26, 2019.
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PilT and PilU are homohexameric ATPases that coordinate to retract type IVa pili
Jennifer L. Chlebek, Hannah Q. Hughes, Aleksandra S. Ratkiewicz, Rasman Rayyan, Joseph Che-Yen Wang, Brittany E. Herrin, Triana N. Dalia, Nicolas Biais, Ankur B. Dalia
bioRxiv 634048; doi: https://doi.org/10.1101/634048
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PilT and PilU are homohexameric ATPases that coordinate to retract type IVa pili
Jennifer L. Chlebek, Hannah Q. Hughes, Aleksandra S. Ratkiewicz, Rasman Rayyan, Joseph Che-Yen Wang, Brittany E. Herrin, Triana N. Dalia, Nicolas Biais, Ankur B. Dalia
bioRxiv 634048; doi: https://doi.org/10.1101/634048

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