PilN binding modulates the structure and binding partners of the Pseudomonas aeruginosa type IVa pilus protein PilM

McCallum, Matthew; Tammam, Stephanie; Little, Dustin J.; Robinson, Howard; Koo, Jason; Shah, Megha; Calmettes, Charles; Moraes, Trevor F.; Burrows, Lori L.; Howell, P. Lynne

doi:10.1074/jbc.M116.718353

Title: PilN binding modulates the structure and binding partners of the Pseudomonas aeruginosa type IVa pilus protein PilM

Journal Article · Mon Mar 28 00:00:00 EDT 2016 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.M116.718353· OSTI ID:1340346

McCallum, Matthew ^[1]; Tammam, Stephanie ^[2]; Little, Dustin J. ^[1]; Robinson, Howard ^[3]; Koo, Jason ^[2]; Shah, Megha ^[4]; Calmettes, Charles ^[4]; Moraes, Trevor F. ^[4]; Burrows, Lori L. ^[5]; Howell, P. Lynne ^[1]

Univ. of Toronto, Toronto, ON (Canada); Hospital for Sick Children, Toronto, ON (Canada)
Hospital for Sick Children, Toronto, ON (Canada)
Brookhaven National Lab. (BNL), Upton, NY (United States)
Univ. of Toronto, Toronto, ON (Canada)
McMaster Univ., Hamilton, ON (Canada); Hospital for Sick Children, Toronto, ON (Canada)

Pseudomonas aeruginosa is an opportunistic bacterial pathogen that expresses type IVa pili. The pilus assembly system, which promotes surface-associated twitching motility and virulence, is composed of inner and outer membrane subcomplexes, connected by an alignment subcomplex composed of PilMNOP. PilM binds to the N terminus of PilN, and we hypothesize that this interaction causes functionally significant structural changes in PilM. To characterize this interaction, we determined the crystal structures of PilM and a PilM chimera where PilM was fused to the first 12 residues of PilN (PilM·PilN(1–12)). Structural analysis, multiangle light scattering coupled with size exclusion chromatography, and bacterial two-hybrid data revealed that PilM forms dimers mediated by the binding of a novel conserved motif in the N terminus of PilM, and binding PilN abrogates this binding interface, resulting in PilM monomerization. Structural comparison of PilM with PilM·PilN(1–12) revealed that upon PilN binding, there is a large domain closure in PilM that alters its ATP binding site. Using biolayer interferometry, we found that the association rate of PilN with PilM is higher in the presence of ATP compared with ADP. Bacterial two-hybrid data suggested the connectivity of the cytoplasmic and inner membrane components of the type IVa pilus machinery in P. aeruginosa, with PilM binding to PilB, PilT, and PilC in addition to PilN. Pull-down experiments demonstrated direct interactions of PilM with PilB and PilT. As a result, we propose a working model in which dynamic binding of PilN facilitates functionally relevant structural changes in PilM.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC00112704

OSTI ID:: 1340346

Report Number(s):: BNL-112064-2016-JA

Journal Information:: Journal of Biological Chemistry, Vol. 291, Issue 21; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 29 works

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Title: PilN binding modulates the structure and binding partners of the Pseudomonas aeruginosa type IVa pilus protein PilM

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