Characterisation of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria

Atack, John M., Srikhanta, Yogitha N., Djoko, Karrera Y., Welch, Jessica P., Hasri, Norain H. M., Steichen, Christopher T., Vanden Hoven, Rachel N., Grimmond, Sean M., Othman, Dk Seti Maimonah Pg, Kappler, Ulrike, Apicella, Michael A., Jennings, Michael P., Edwards, Jennifer L. and McEwan, Alastair G. (2013) Characterisation of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria. Journal of Bacteriology, 195 11: 2632-2641. doi:10.1128/JB.02062-12

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Author Atack, John M.
Srikhanta, Yogitha N.
Djoko, Karrera Y.
Welch, Jessica P.
Hasri, Norain H. M.
Steichen, Christopher T.
Vanden Hoven, Rachel N.
Grimmond, Sean M.
Othman, Dk Seti Maimonah Pg
Kappler, Ulrike
Apicella, Michael A.
Jennings, Michael P.
Edwards, Jennifer L.
McEwan, Alastair G.
Title Characterisation of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria
Formatted title
Characterisation of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
1067-8832
Publication date 2013-06-01
Year available 2013
Sub-type Article (original research)
DOI 10.1128/JB.02062-12
Open Access Status File (Author Post-print)
Volume 195
Issue 11
Start page 2632
End page 2641
Total pages 10
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2014
Language eng
Formatted abstract
NtrYX is a sensor-histidine kinase/response regulator two-component system that has had limited characterization in a small number of Alphaproteobacteria. Phylogenetic analysis of the response regulator NtrX showed that this two-component system is extensively distributed across the bacterial domain, and it is present in a variety of Betaproteobacteria, including the human pathogen Neisseria gonorrhoeae. Microarray analysis revealed that the expression of several components of the respiratory chain was reduced in an N. gonorrhoeae ntrX mutant compared to that in the isogenic wild-type (WT) strain 1291. These included the cytochrome c oxidase subunit (ccoP), nitrite reductase (aniA), and nitric oxide reductase (norB). Enzyme activity assays showed decreased cytochrome oxidase and nitrite reductase activities in the ntrX mutant, consistent with microarray data. N. gonorrhoeae ntrX mutants had reduced capacity to survive inside primary cervical cells compared to the wild type, and although they retained the ability to form a biofilm, they exhibited reduced survival within the biofilm compared to wild-type cells, as indicated by LIVE/DEAD staining. Analyses of an ntrX mutant in a representative alphaproteobacterium, Rhodobacter capsulatus, showed that cytochrome oxidase activity was also reduced compared to that in the wild-type strain SB1003. Taken together, these data provide evidence that the NtrYX two-component system may be a key regulator in the expression of respiratory enzymes and, in particular, cytochrome c oxidase, across a wide range of proteobacteria, including a variety of bacterial pathogens.
Keyword Cytochrome-c-oxidase
Rhodobacter-capsulatus
Escherichia-voli
Nitric-oxide
Bradyrhizobium-japonicum
Gonococcal biofilms
Signal-transduction
Aerobic regulation
Ubiquinol oxidase
Nitrogen-fixation
α-Proteobacteria
β-Proteobacteria
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published online ahead of print 5 April 2013

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 12 Apr 2013, 20:46:20 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences