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Protein interactions within and between two F-type type IV secretion systems

Lookup NU author(s): Dr Birgit Koch, Jonathan Tellechea Luzardo, Professor Natalio KrasnogorORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. Bacterial type IV secretion systems (T4SSs) can mediate conjugation. The T4SS from Neisseria gonorrhoeae possesses the unique ability to mediate DNA secretion into the extracellular environment. The N. gonorrhoeae T4SS can be grouped with F-type conjugative T4SSs based on homology. We tested 17 proteins important for DNA secretion by N. gonorrhoeae for protein interactions. The BACTH-TM bacterial two-hybrid system was successfully used to study periplasmic interactions. By determining if the same interactions were observed for F-plasmid T4SS proteins and when one interaction partner was replaced by the corresponding protein from the other T4SS, we aimed to identify features associated with the unique function of the N. gonorrhoeae T4SS as well as generic features of F-type T4SSs. For both systems, we observed already described interactions shared by homologs from other T4SSs as well as new and described interactions between F-type T4SS-specific proteins. Furthermore, we demonstrate, for the first-time, interactions between proteins with homology to the conserved T4SS outer membrane core proteins and F-type-specific proteins and we confirmed two of them by co-purification. The F-type-specific protein TraHN was found to localize to the outer membrane and the presence of significant amounts of TraHN in the outer membrane requires TraGN.


Publication metadata

Author(s): Koch B, Callaghan MM, Tellechea-Luzardo J, Seeger AY, Dillard JP, Krasnogor N

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2020

Volume: 114

Issue: 5

Pages: 823-838

Print publication date: 01/11/2020

Online publication date: 01/08/2020

Acceptance date: 20/07/2020

Date deposited: 15/10/2020

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: John Wiley & Sons Ltd

URL: https://doi.org/10.1111/mmi.14582

DOI: 10.1111/mmi.14582

PubMed id: 32738086


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Funding

Funder referenceFunder name
EP/J004111/2,
EP/N031926/1
EPSRC Grant Nos EP/L001489/2
NIH grant R01AI047958 to J.P.D.
Royal Academy of Engineering Chair in Emerging Technology to N.K

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