The distinctive cell division interactome of Neisseria gonorrhoeae
Abstract Background Bacterial cell division is an essential process driven by the formation of a Z-ring structure, as a cytoskeletal scaffold at the mid-cell, followed by the recruitment of various proteins which form the divisome. The cell division interactome reflects the complement of different i...
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doaj-c7c0666a510f4408b563452720b91a5a2020-11-25T01:46:54ZengBMCBMC Microbiology1471-21802017-12-0117111410.1186/s12866-017-1140-1The distinctive cell division interactome of Neisseria gonorrhoeaeYinan Zou0Yan Li1Jo-Anne R. Dillon2Department of Microbiology and Immunology, College of MedicineVaccine and Infectious Disease Organization, International Vaccine CentreDepartment of Microbiology and Immunology, College of MedicineAbstract Background Bacterial cell division is an essential process driven by the formation of a Z-ring structure, as a cytoskeletal scaffold at the mid-cell, followed by the recruitment of various proteins which form the divisome. The cell division interactome reflects the complement of different interactions between all divisome proteins. To date, only two cell division interactomes have been characterized, in Escherichia coli and in Streptococcus pneumoniae. The cell divison proteins encoded by Neisseria gonorrhoeae include FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsI, FtsW, and FtsN. The purpose of the present study was to characterize the cell division interactome of N. gonorrhoeae using several different methods to identify protein-protein interactions. We also characterized the specific subdomains of FtsA implicated in interactions with FtsZ, FtsQ, FtsN and FtsW. Results Using a combination of bacterial two-hybrid (B2H), glutathione S-transferase (GST) pull-down assays, and surface plasmon resonance (SPR), nine interactions were observed among the eight gonococcal cell division proteins tested. ZipA did not interact with any other cell division proteins. Comparisons of the N. gonorrhoeae cell division interactome with the published interactomes from E. coli and S. pneumoniae indicated that FtsA-FtsZ and FtsZ-FtsK interactions were common to all three species. FtsA-FtsW and FtsK-FtsN interactions were only present in N. gonorrhoeae. The 2A and 2B subdomains of FtsANg were involved in interactions with FtsQ, FtsZ, and FtsN, and the 2A subdomain was involved in interaction with FtsW. Conclusions Results from this research indicate that N. gonorrhoeae has a distinctive cell division interactome as compared with other microorganisms.http://link.springer.com/article/10.1186/s12866-017-1140-1Cell divisionInteractomeN. gonorrhoeaeProtein-protein interactionBacterial two-hybrid assaySurface plasmon resonance |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yinan Zou Yan Li Jo-Anne R. Dillon |
spellingShingle |
Yinan Zou Yan Li Jo-Anne R. Dillon The distinctive cell division interactome of Neisseria gonorrhoeae BMC Microbiology Cell division Interactome N. gonorrhoeae Protein-protein interaction Bacterial two-hybrid assay Surface plasmon resonance |
author_facet |
Yinan Zou Yan Li Jo-Anne R. Dillon |
author_sort |
Yinan Zou |
title |
The distinctive cell division interactome of Neisseria gonorrhoeae |
title_short |
The distinctive cell division interactome of Neisseria gonorrhoeae |
title_full |
The distinctive cell division interactome of Neisseria gonorrhoeae |
title_fullStr |
The distinctive cell division interactome of Neisseria gonorrhoeae |
title_full_unstemmed |
The distinctive cell division interactome of Neisseria gonorrhoeae |
title_sort |
distinctive cell division interactome of neisseria gonorrhoeae |
publisher |
BMC |
series |
BMC Microbiology |
issn |
1471-2180 |
publishDate |
2017-12-01 |
description |
Abstract Background Bacterial cell division is an essential process driven by the formation of a Z-ring structure, as a cytoskeletal scaffold at the mid-cell, followed by the recruitment of various proteins which form the divisome. The cell division interactome reflects the complement of different interactions between all divisome proteins. To date, only two cell division interactomes have been characterized, in Escherichia coli and in Streptococcus pneumoniae. The cell divison proteins encoded by Neisseria gonorrhoeae include FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsI, FtsW, and FtsN. The purpose of the present study was to characterize the cell division interactome of N. gonorrhoeae using several different methods to identify protein-protein interactions. We also characterized the specific subdomains of FtsA implicated in interactions with FtsZ, FtsQ, FtsN and FtsW. Results Using a combination of bacterial two-hybrid (B2H), glutathione S-transferase (GST) pull-down assays, and surface plasmon resonance (SPR), nine interactions were observed among the eight gonococcal cell division proteins tested. ZipA did not interact with any other cell division proteins. Comparisons of the N. gonorrhoeae cell division interactome with the published interactomes from E. coli and S. pneumoniae indicated that FtsA-FtsZ and FtsZ-FtsK interactions were common to all three species. FtsA-FtsW and FtsK-FtsN interactions were only present in N. gonorrhoeae. The 2A and 2B subdomains of FtsANg were involved in interactions with FtsQ, FtsZ, and FtsN, and the 2A subdomain was involved in interaction with FtsW. Conclusions Results from this research indicate that N. gonorrhoeae has a distinctive cell division interactome as compared with other microorganisms. |
topic |
Cell division Interactome N. gonorrhoeae Protein-protein interaction Bacterial two-hybrid assay Surface plasmon resonance |
url |
http://link.springer.com/article/10.1186/s12866-017-1140-1 |
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