Electron Cryotomography of Mycoplasma pneumoniae Mutants Correlates Terminal Organelle Architectural Features and Function
Abstract
The Mycoplasma pneumoniae terminal organelle functions in adherence and gliding motility and is comprised of at least eleven substructures. We used electron cryotomography to correlate impaired gliding and adherence function with changes in architecture in diverse terminal organelle mutants. All eleven substructures were accounted for in the prkC, prpC, and P200 mutants, and variably so for the HMW3 mutant. Conversely, no terminal organelle substructures were evident in HMW1 and HMW2 mutants. The P41 mutant exhibits a terminal organelle detachment phenotype and lacked the bowl element normally present at the terminal organelle base. Complementation restored this substructure, establishing P41 as either a component of the bowl element or required for its assembly or stability, and that this bowl element is essential to anchor the terminal organelle but not for leverage in gliding. Mutants II-3, III-4, and topJ exhibited a visibly lower density of protein knobs on the terminal organelle surface. Mutants II-3 and III-4 lack accessory proteins required for a functional adhesin complex, while the topJ mutant lacks a DnaJ-like co-chaperone essential for its assembly. Taken together, these observations expand our understanding of the roles of certain terminal organelle proteins in the architecture and function of this complex structure.
Additional Information
© 2018 John Wiley & Sons Ltd. Accepted manuscript online: 22 Feb 2018. Manuscript Accepted: 20 Feb 2018. Manuscript Revised: 19 Feb 2018. Manuscript Received: 24 Oct 2017. Issue Online 23 April 2018. This work was supported by Public Health Service research grants AI49194 and AI110098 from the National Institute of Allergy and Infectious Diseases to D.C.K. We acknowledge Mitch Balish for helpful discussions. We declare no competing interests. AUTHOR CONTRIBUTIONS: Study conception and design: D.C.K. and G.J.J.; data acquisition and analysis: D.C.K., S.C., J.S., A.J., E.S.S., and G.J.J.; writing the manuscript: D.C.K., S.C., and G.J.J.Attached Files
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Additional details
- PMCID
- PMC5912986
- Eprint ID
- 84961
- Resolver ID
- CaltechAUTHORS:20180227-074921090
- AI49194
- NIH
- AI110098
- NIH
- National Institute of Allergy and Infectious Diseases
- Created
-
2018-02-27Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field