Regulation of minD by oxyR in Neisseria gonorrhoeae

Parti, Rajinder P.; Horbay, Monique A.; Liao, Mingmin; Dillon, Jo-Anne R.

doi:10.1016/j.resmic.2013.02.002

Cited by 11 publications

(7 citation statements)

References 43 publications

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“…Moreover, MinD of Spec R was shifted to a more acidic pI and also increased in response to the higher subMIC. MinD plays a crucial role in a division site selection process and in stress response in N. gonorrhoeae (Szeto et al , 2001; Parti et al , 2013). Our results from microscopic examination revealed that no morphological difference existed between the susceptible and resistant strains (Fig.…”

Section: Discussionmentioning

confidence: 99%

Reference map and comparative proteomic analysis of Neisseria gonorrhoeae displaying high resistance against spectinomycin

Nabu

Lawung

Isarankura-Na-Ayudhya

et al. 2014

Journal of Medical Microbiology

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A proteome reference map of Neisseria gonorrhoeae was successfully established using twodimensional gel electrophoresis in conjunction with matrix-assisted laser desorption ionizationtime of flight mass spectrometry. This map was further applied to compare protein expression profiles of high-level spectinomycin-resistant (clinical isolate) and -susceptible (reference strain) N. gonorrhoeae following treatment with subminimal inhibitory concentrations (subMICs) of spectinomycin. Approximately 200 protein spots were visualized by Coomassie brilliant blue G-250 staining and 66 spots representing 58 unique proteins were subsequently identified. Most of the identified proteins were analysed as cytoplasmic proteins and belonged to the class of energy metabolism. Comparative proteomic analysis of whole protein expression of susceptible and resistant gonococci showed up to 96 % similarity while eight proteins were found to be differentially expressed in the resistant strain. In the presence of subMICs of spectinomycin, it was found that 50S ribosomal protein L7/L12, an essential component for ribosomal translocation, was upregulated in both strains, ranging from 1.5-to 3.5-fold, suggesting compensatory mechanisms of N. gonorrhoeae in response to antibiotic that inhibits protein synthesis. Moreover, the differential expression of proteins involved in energy metabolism, amino acid biosynthesis, and the cell envelope was noticeably detected, indicating significant cellular responses and adaptation against antibiotic stress. Such knowledge provides valuable data, not only fundamental proteomic data, but also knowledge of the mode of action of antibiotic and secondary target proteins implicated in adaptation and compensatory mechanisms.

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Section: Discussionmentioning

confidence: 99%

Reference map and comparative proteomic analysis of Neisseria gonorrhoeae displaying high resistance against spectinomycin

Nabu

Lawung

Isarankura-Na-Ayudhya

et al. 2014

Journal of Medical Microbiology

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“…The upstream region of orf20 may contain a DepR-binding region based on the previous research on OxyR, the homologue of DepR in N . gonorrheae [ 7 ]. Initially a 401-bp DNA fragment carrying the 26-bp orf20 - orf21 intergenic region ( Fig 1A ) was obtained by PCR amplification using the primer pair XJ59F/XJ59R.…”

Section: Resultsmentioning

confidence: 99%

“…In Neisseria gonorrhoeae , the min operon is composed of four genes, minCDE and a LysR-type transcriptional regulator (LTTR) gene oxyR . OxyR regulates the expression of minD [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Mechanistic studies of DepR in regulating FK228 biosynthesis in Chromobacterium violaceum no. 968

et al. 2018

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DepR, a LysR-type transcriptional regulator encoded by the last gene of the putative min operon (orf21-20-19-depR) located at the downstream region of the anticancer agent FK228 biosynthetic gene cluster in Chromobacterium violaceum No. 968, positively regulates the biosynthesis of FK228. In this work, the mechanism underlining this positive regulation was probed by multiple approaches. Electrophoretic mobility shift assay (EMSA) and DNase I footprinting assay (DIFA) identified a conserved 35-nt DNA segment in the orf21-orf22 intergenic region where the purified recombinant DepR binds to. Quantitative reverse transcription PCR (RT-qPCR) and green fluorescent protein (GFP) promoter probe assays established that transcription of phasin gene orf22 increases in the depR deletion mutant of C. violaceum (CvΔdepR) compared to the wild-type strain. FK228 production in the orf22-overexpressed strain C. violaceum was reduced compared with the wild-type strain. DepR has two conserved cysteine residues C199 and C208 presumed to form a disulfide bridge upon sensing oxidative stress. C199X point mutations that locked DepR in a reduced conformation decreased the DNA-binding affinity of DepR; T232A or R278A mutation also had a negative impact on DNA binding of DepR. Complementation of CvΔdepR with any of those versions of depR carrying a single codon mutation was not able to restore FK228 production to the level of wild-type strain. All evidences collectively suggested that DepR positively regulates the biosynthesis of FK228 through indirect metabolic networking.

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“…For three out of seven genes in operons ( S1 Table ) this symmetry was found [ 30 ]. Interestingly, this was not the case for minC and oxyR although OxyR negatively regulates the promoter in the minCDE-oxyR gene cluster [ 31 ]. OxyR, a regulator for the expression of catalase [ 32 ], is overexpressed in NmΔ dinG under the MMC stress condition.…”

Section: Discussionmentioning

confidence: 99%

The helicase DinG responds to stress due to DNA double strand breaks

et al. 2017

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Neisseria meningitidis (Nm) is a Gram-negative nasopharyngeal commensal that can cause septicaemia and meningitis. The neisserial DNA damage-inducible protein DinG is a helicase related to the mammalian helicases XPD and FANCJ. These helicases belong to superfamily 2, are ATP dependent and exert 5′ → 3′ directionality. To better understand the role of DinG in neisserial genome maintenance, the Nm DinG (DinGNm) enzymatic activities were assessed in vitro and phenotypical characterization of a dinG null mutant (NmΔdinG) was performed. Like its homologues, DinGNm possesses 5′ → 3′ directionality and prefers DNA substrates containing a 5′-overhang. ATPase activity of DinGNm is strictly DNA-dependent and DNA unwinding activity requires nucleoside triphosphate and divalent metal cations. DinGNm directly binds SSBNm with a Kd of 313 nM. Genotoxic stress analysis demonstrated that NmΔdinG was more sensitive to double-strand DNA breaks (DSB) induced by mitomycin C (MMC) than the Nm wildtype, defining the role of neisserial DinG in DSB repair. Notably, when NmΔdinG cells grown under MMC stress assessed by quantitative mass spectrometry, 134 proteins were shown to be differentially abundant (DA) compared to unstressed NmΔdinG cells. Among the DNA replication, repair and recombination proteins affected, polymerase III subunits and recombinational repair proteins RuvA, RuvB, RecB and RecD were significantly down regulated while TopA and SSB were upregulated under stress condition. Most of the other DA proteins detected are involved in metabolic functions. The present study shows that the helicase DinG is probably involved in regulating metabolic pathways as well as in genome maintenance.

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Regulation of minD by oxyR in Neisseria gonorrhoeae

Cited by 11 publications

References 43 publications

Reference map and comparative proteomic analysis of Neisseria gonorrhoeae displaying high resistance against spectinomycin

Reference map and comparative proteomic analysis of Neisseria gonorrhoeae displaying high resistance against spectinomycin

Mechanistic studies of DepR in regulating FK228 biosynthesis in Chromobacterium violaceum no. 968

The helicase DinG responds to stress due to DNA double strand breaks

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