Architecture of the type IVa pilus machine
Abstract
Many bacteria, including important pathogens, move by projecting grappling-hook–like extensions called type IV pili from their cell bodies. After these pili attach to other cells or objects in their environment, the bacteria retract the pili to pull themselves forward. Chang et al. used electron cryotomography of intact cells to image the protein machines that extend and retract the pili, revealing where each protein component resides. Putting the known structures of the individual proteins in place like pieces of a three-dimensional puzzle revealed insights into how the machine works, including evidence that ATP hydrolysis by cytoplasmic motors rotates a membrane-embedded adaptor that slips pilin subunits back and forth from the membrane onto the pilus.
Additional Information
© 2016 American Association for the Advancement of Science. Received 10 August 2015; accepted 13 January 2016. We thank C. Oikonomou and D. Ortega for discussions. Supported by NIH grant R01 GM094800B (G.J.J.), the Howard Hughes Medical Institute, the Max Planck Society, and the Deutsche Forschungsgemeinschaft within the framework of the Collaborative Research Center (SFB) 987 "Microbial Diversity in Environmental Signal Response." The 18 subtomogram averages of T4PMs reported in this study have been deposited in the Electron Microscopy Data Bank with accession numbers EMD-3247 (wild type, piliated); EMD-3248 (wild type, empty); EMD-3249 (ΔpilP, empty); EMD-3250 (PilP-sfGFP, piliated); EMD-3251 (PilP-sfGFP, empty); EMD-3252 (ΔtsaP, piliated); EMD-3253 (ΔtsaP, empty); EMD-3254 (PilO-sfGFP, piliated); EMD-3255 (PilO-sfGFP, empty); EMD-3256 (ΔpilC, empty); EMD-3257 (ΔpilA, empty); EMD-3258 (ΔpilV pilW fimU 1+2+3, empty); EMD-3259 (ΔpilT, piliated); EMD-3260 (ΔpilB, empty); EMD-3261 (ΔpilB ΔpilT, empty); EMD-3262 (ΔpilM, empty); EMD-3263 (ΔpilQβ1-β2, piliated); and EMD-3264 (ΔpilQβ1-β2, empty). The coordinates of the hypothetical T4PM working models have been deposited in the Protein Data Bank with accession numbers 3JC8 (piliated) and 3JC9 (empty), respectively. Author contributions: Y.-W.C. collected the cryo–electron tomography data, which were analyzed by Y.-W.C. and L.A.R.; Y.-W.C. built the T4PM models and generated the movie describing the modeling process; A.T.-L. and L.S.-A. provided the M. xanthus strains and characterized their motility and T4PM component accumulation and localization; J.I. produced the animation of T4PM dynamics; and Y.-W.C., L.S.-A., and G.J.J. wrote the paper.Attached Files
Accepted Version - nihms962793.pdf
Supplemental Material - Chang.SM.pdf
Supplemental Material - aad2001s1.mov
Supplemental Material - aad2001s2.mov
Supplemental Material - aad2001s3.mov
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Additional details
- PMCID
- PMC5929464
- Eprint ID
- 65350
- Resolver ID
- CaltechAUTHORS:20160315-090327567
- R01 GM094800B
- NIH
- Howard Hughes Medical Institute (HHMI)
- Max Planck Society
- Deutsche Forschungsgemeinschaft (DFG)
- Created
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2016-03-15Created from EPrint's datestamp field
- Updated
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2023-06-01Created from EPrint's last_modified field