CryoEM structure of the Vibrio cholerae Type IV competence pilus secretin PilQ

Weaver, Sara J.; Sazinsky, Matthew H.; Dalia, Triana N.; Jensen, Grant J.

doi:10.1101/2020.03.03.975896

Cited by 2 publications

(1 citation statement)

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“…PilQ secretins from Proteobacteria, structurally characterized at low resolution, show radial spokes emerging from a central barrel [16][17][18][19] . Models of PilQ from Thermus thermophilus (PilQ Tt ) and Vibrio cholerae (PilQ Vc ) competence pilus systems -which are divergent from Proteobacterial T4aP secretins -were recently built into 7 and 2.7 Å resolution electron cryomicroscopy (cryoEM) maps, respectively 20,21 . These competence secretins lack the lip subdomain and the radial spokes found in T4aP secretins.…”

Section: Introductionmentioning

confidence: 99%

CryoEM map ofPseudomonas aeruginosaPilQ enables structural characterization of TsaP

McCallum

Tammam

Rubinstein

et al. 2020

Preprint

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19The type IV pilus machinery is a multi-protein complex that polymerizes and 20 depolymerizes a pilus fibre used for attachment, twitching motility, phage adsorption, natural 21 competence, protein secretion, and surface-sensing. An outer membrane secretin pore is required 22 for passage of the pilus fibre out of the cell. Herein, the structure of the tetradecameric secretin, 23PilQ, from the Pseudomonas aeruginosa type IVa pilus was determined to 4.3 Å resolution in the 24 presence and absence of C7 symmetric spokes. The heptameric spokes were found to be the two 25 tandem C-terminal domains of TsaP. TsaP forms a belt around PilQ and while the protein is not 26 essential for PilQ assembly, over-expression of TsaP triggers the surface-sensing signal cascade 27 upstream of PilY1, leading to cyclic di-GMP up-regulation. These results resolve the identity of 28 the spokes identified with Proteobacterial PilQ and may reveal a new component of the surface-29 sensing cyclic di-GMP signal cascade. 30 31

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