TY - JOUR
T1 - Acinetobacter baylyi regulates type IV pilus synthesis by employing two extension motors and a motor protein inhibitor
AU - Ellison, Courtney K.
AU - Dalia, Triana N.
AU - Klancher, Catherine A.
AU - Shaevitz, Joshua W.
AU - Gitai, Zemer
AU - Dalia, Ankur B.
N1 - Funding Information:
We would like to thank E. Geisinger for A. baylyi ADP1 ATCC33305 wildtype strain, and X. Charpentier for the apramycin resistance cassette. We would like to thank K. Hummels and B. Bratton for helpful suggestions on phylogenetic analysis. C. K. E. is a Damon Runyon Fellow supported by the Damon Runyon Cancer Research Foundation (DRG-2385-20). This work was supported in part by the National Science Foundation, through the Center for the Physics of Biological Function (PHY-1734030). This work was supported by grant R35GM128674 from the National Institutes of Health awarded to A. B. D. and the National Institutes of Health Pioneer Award 1DP1AI124669-01 awarded to Z. G.
Publisher Copyright:
© 2021, The Author(s).
PY - 2021/12/1
Y1 - 2021/12/1
N2 - Bacteria use extracellular appendages called type IV pili (T4P) for diverse behaviors including DNA uptake, surface sensing, virulence, protein secretion, and twitching motility. Dynamic extension and retraction of T4P is essential for their function, and T4P extension is thought to occur through the action of a single, highly conserved motor, PilB. Here, we develop Acinetobacter baylyi as a model to study T4P by employing a recently developed pilus labeling method. By contrast to previous studies of other bacterial species, we find that T4P synthesis in A. baylyi is dependent not only on PilB but also on an additional, phylogenetically distinct motor, TfpB. Furthermore, we identify a protein (CpiA) that inhibits T4P extension by specifically binding and inhibiting PilB but not TfpB. These results expand our understanding of T4P regulation and highlight how inhibitors might be exploited to disrupt T4P synthesis.
AB - Bacteria use extracellular appendages called type IV pili (T4P) for diverse behaviors including DNA uptake, surface sensing, virulence, protein secretion, and twitching motility. Dynamic extension and retraction of T4P is essential for their function, and T4P extension is thought to occur through the action of a single, highly conserved motor, PilB. Here, we develop Acinetobacter baylyi as a model to study T4P by employing a recently developed pilus labeling method. By contrast to previous studies of other bacterial species, we find that T4P synthesis in A. baylyi is dependent not only on PilB but also on an additional, phylogenetically distinct motor, TfpB. Furthermore, we identify a protein (CpiA) that inhibits T4P extension by specifically binding and inhibiting PilB but not TfpB. These results expand our understanding of T4P regulation and highlight how inhibitors might be exploited to disrupt T4P synthesis.
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U2 - 10.1038/s41467-021-24124-6
DO - 10.1038/s41467-021-24124-6
M3 - Article
C2 - 34145281
AN - SCOPUS:85108154858
SN - 2041-1723
VL - 12
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 3744
ER -