RosR (Cg1324), a Hydrogen Peroxide-sensitive MarR-type Transcriptional Regulator of Corynebacterium glutamicum*

Bußmann, Michael; Baumgart, Meike; Bott, Michael

doi:10.1074/jbc.m110.156372

Cited by 53 publications

(40 citation statements)

References 59 publications

(65 reference statements)

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“…The gels were stained with a Coomassie dye based RAPIDstain solution (G-Biosciences, St. Louis, MO, USA). MALDI-TOF-MS measurements were performed with an Ultraflex III TOF/TOF mass spectrometer (Bruker Daltonics, Bremen, Germany) for the identification of the proteins as described (38). …”

Section: Methodsmentioning

confidence: 99%

Silencing of cryptic prophages inCorynebacterium glutamicum

et al. 2016

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DNA of viral origin represents a ubiquitous element of bacterial genomes. Its integration into host regulatory circuits is a pivotal driver of microbial evolution but requires the stringent regulation of phage gene activity. In this study, we describe the nucleoid-associated protein CgpS, which represents an essential protein functioning as a xenogeneic silencer in the Gram-positive Corynebacterium glutamicum. CgpS is encoded by the cryptic prophage CGP3 of the C. glutamicum strain ATCC 13032 and was first identified by DNA affinity chromatography using an early phage promoter of CGP3. Genome-wide profiling of CgpS binding using chromatin affinity purification and sequencing (ChAP-Seq) revealed its association with AT-rich DNA elements, including the entire CGP3 prophage region (187 kbp), as well as several other elements acquired by horizontal gene transfer. Countersilencing of CgpS resulted in a significantly increased induction frequency of the CGP3 prophage. In contrast, a strain lacking the CGP3 prophage was not affected and displayed stable growth. In a bioinformatics approach, cgpS orthologs were identified primarily in actinobacterial genomes as well as several phage and prophage genomes. Sequence analysis of 618 orthologous proteins revealed a strong conservation of the secondary structure, supporting an ancient function of these xenogeneic silencers in phage-host interaction.

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Section: Methodsmentioning

confidence: 99%

Silencing of cryptic prophages inCorynebacterium glutamicum

et al. 2016

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“…The PCR products were cloned into TOPO pCR2.1 (Invitrogen) and sequenced. Primer extension analysis was performed as described previously (16). Reverse transcription was carried out with a volume of 20 l using 20 g total RNA, 400 U Superscript III reverse transcriptase (Invitrogen), 5 nM primer (5=-FAM [6-carboxyfluorescein]-CATAGGCGAAGACCGTGTAGATCCCGAC-3=), and 750 M dATP, dCTP, dTTP, and dGTP at 55°C for 1.5 h. The reverse transcription reaction was repeated as described previously (26).…”

Section: Methodsmentioning

confidence: 99%

“…MA1 encodes a transcriptional regulator that shares 62% amino acid identity with the regulatory protein MarR (multiple-antibiotic-resistance regulator) from Gordonia bronchialis DSM 43247 (NCBI accession number YP_003274556). The MarR family of proteins is involved in environmental stress responses and in the catabolic pathways of aromatic compounds (16) and is known to bind a number of anionic lipophilic, and often phenolic, effector molecules (17). MarR is also reported to negatively regulate a small cluster of naphthalene catabolism-related genes called nagR2-ORF2IЉKL in the naphthalene-degrading bacterium Polaromonas naphthalenivorans CJ2 (18) and the marRAB operon in Escherichia coli (19).…”

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confidence: 99%

Analysis of the xplAB -Containing Gene Cluster Involved in the Bacterial Degradation of the Explosive Hexahydro-1,3,5-Trinitro-1,3,5-Triazine

Chong

Sabir

Lorenz

et al. 2014

Appl Environ Microbiol

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c Repeated use of the explosive compound hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) on military land has resulted in significant soil and groundwater pollution. Rates of degradation of RDX in the environment are low, and accumulated RDX, which the U.S. Environmental Protection Agency has determined is a possible human carcinogen, is now threatening drinking water supplies. RDX-degrading microorganisms have been isolated from RDX-contaminated land; however, despite the presence of these species in contaminated soils, RDX pollution persists. To further understand this problem, we studied RDX-degrading species belonging to four different genera (Rhodococcus, Microbacterium, Gordonia, and Williamsia) isolated from geographically distinct locations and established that the xplA and xplB (xplAB) genes, which encode a cytochrome P450 and a flavodoxin redox partner, respectively, are nearly identical in all these species. Together, the xplAB system catalyzes the reductive denitration of RDX and subsequent ring cleavage under aerobic and anaerobic conditions. In addition to xplAB, the Rhodococcus species studied here share a 14-kb region flanking xplAB; thus, it appears likely that the RDX-metabolizing ability was transferred as a genomic island within a transposable element. The conservation and transfer of xplAB-flanking genes suggest a role in RDX metabolism. We therefore independently knocked out genes within this cluster in the RDX-degrading species Rhodococcus rhodochrous 11Y. Analysis of the resulting mutants revealed that XplA is essential for RDX degradation and that XplB is not the sole contributor of reducing equivalents to XplA. While XplA expression is induced under nitrogen-limiting conditions and further enhanced by the presence of RDX, MarR is not regulated by RDX.

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“…The present analysis of gene expression in the arnR-deficient strain also indicates that the narK gene is downregulated in response to supplementation with nitrite or NO under anaerobic conditions. It should be noted that in addition to ArnR and GlxR, two other regulators, RipA (42) and RosR (43), are involved in the expression of the narKGHJI operon in C. glutamicum. RipA is an AraCtype regulator that represses the narKGHJI operon under conditions of iron limitation.…”

Section: Discussionmentioning

confidence: 99%

Corynebacterium glutamicum ArnR Controls Expression of Nitrate Reductase Operon narKGHJI and Nitric Oxide (NO)-Detoxifying Enzyme Gene hmp in an NO-Responsive Manner

Nishimura

Teramoto

Inui

et al. 2013

Journal of Bacteriology

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Corynebacterium glutamicum ArnR is a novel transcriptional regulator that represses expression of the nitrate reductase operon narKGHJI and the nitric oxide (NO)-detoxifying flavohemoglobin gene hmp under aerobic conditions. In a previous study, we showed that ArnR-mediated repression is relieved during anaerobic nitrate respiration, but we could not pinpoint the specific signal that ArnR senses. In this study, we show that in the absence of nitrate, ArnR-mediated repression is maintained under anaerobic conditions. The derepression in response to nitrate is eliminated by disruption of narG, suggesting that ArnR senses nitrate derivatives generated during nitrate respiration. Specifically, the hmp gene is upregulated in the presence of nitrite or nitric oxide (NO) in an ArnR-dependent manner, although the response of narK appears to be greatly affected by ArnR-independent regulation. In vitro binding of ArnR to the narK and hmp promoter regions is more strongly inhibited by NO than by nitrite. We previously showed that the UV-visible spectrum of ArnR is typical of a Fe-S cluster-containing protein. Site-directed mutagenesis of each of three cysteine residues, which are possibly involved in coordination of the cofactor in the ArnR protein, results in loss of the binding of this protein to its target promoters in vitro and eliminates the repression of the target genes in vivo under aerobic conditions. These observations suggest that the cofactor coordinated by these three cysteine residues in the ArnR protein plays a critical role in the NO-responsive expression of the narKGHJI operon and the hmp gene.

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RosR (Cg1324), a Hydrogen Peroxide-sensitive MarR-type Transcriptional Regulator of Corynebacterium glutamicum*

Cited by 53 publications

References 59 publications

Silencing of cryptic prophages inCorynebacterium glutamicum

Silencing of cryptic prophages inCorynebacterium glutamicum

Analysis of the xplAB -Containing Gene Cluster Involved in the Bacterial Degradation of the Explosive Hexahydro-1,3,5-Trinitro-1,3,5-Triazine

Corynebacterium glutamicum ArnR Controls Expression of Nitrate Reductase Operon narKGHJI and Nitric Oxide (NO)-Detoxifying Enzyme Gene hmp in an NO-Responsive Manner

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