Zoellner, Robert, Cronenberg, Tom and Maier, Berenike ORCID: 0000-0001-6971-9927 (2019). Motor Properties of PilT-Independent Type 4 Pilus Retraction in Gonococci. J. Bacteriol., 201 (18). WASHINGTON: AMER SOC MICROBIOLOGY. ISSN 1098-5530
Full text not available from this repository.Abstract
Bacterial type 4 pili (T4P) belong to the strongest molecular machines. The gonococcal T4P retraction ATPase PilT supports forces exceeding 100 pN during T4P retraction. Here, we address the question of whether gonococcal T4P retract in the absence of PilT. We show that pilT deletion strains indeed retract their T4P, but the maximum force is reduced to 5 pN. Similarly, the speed of T4P retraction is lower by orders of magnitude compared to that of T4P retraction driven by PilT. Deleting the pilT paralogue pilT2 further reduces the speed of T4P retraction, yet T4P retraction is detectable in the absence of all three pilT paralogues. Furthermore, we show that depletion of proton motive force (PMF) slows but does not inhibit pilT-independent T4P retraction. We conclude that the retraction ATPase is not essential for gonococcal T4P retraction. However, the force generated in the absence of PilT is too low to support important functions of T4P, including twitching motility, fluidization of colonies, and induction of host cell response. IMPORTANCE Bacterial type 4 pili (T4P) have been termed the Swiss Army knives of bacteria because they perform numerous functions, including host cell interaction, twitching motility, colony formation, DNA uptake, protein secretion, and surface sensing. The pilus fiber continuously elongates or retracts, and these dynamics are functionally important. Curiously, only a subset of T4P systems employ T4P retraction ATPases to power T4P retraction. Here, we show that one of the strongest T4P machines, the gonococcal T4P, retracts without a retraction ATPase. Biophysical characterization reveals strongly reduced force and speed compared to retraction with ATPase. We propose that bacteria encode retraction ATPases when T4P have to generate high-force-supporting functions like twitching motility, triggering host cell response, or fluidizing colonies.
Item Type: | Journal Article | ||||||||||||||||
Creators: |
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URN: | urn:nbn:de:hbz:38-143458 | ||||||||||||||||
DOI: | 10.1128/JB.00778-18 | ||||||||||||||||
Journal or Publication Title: | J. Bacteriol. | ||||||||||||||||
Volume: | 201 | ||||||||||||||||
Number: | 18 | ||||||||||||||||
Date: | 2019 | ||||||||||||||||
Publisher: | AMER SOC MICROBIOLOGY | ||||||||||||||||
Place of Publication: | WASHINGTON | ||||||||||||||||
ISSN: | 1098-5530 | ||||||||||||||||
Language: | English | ||||||||||||||||
Faculty: | Faculty of Mathematics and Natural Sciences | ||||||||||||||||
Divisions: | Faculty of Mathematics and Natural Sciences > Department of Physics > Institut für Biologische Physik | ||||||||||||||||
Subjects: | no entry | ||||||||||||||||
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Refereed: | Yes | ||||||||||||||||
URI: | http://kups.ub.uni-koeln.de/id/eprint/14345 |
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