The flavohemoglobin BCFHG1 is the main NO detoxification system and confers protection against nitrosative conditions but is not a virulence factor in the fungal necrotroph Botrytis cinerea

Turrion-Gomez, Juan Luis; Eslava, Arturo P.; Benito, Ernesto P.

doi:10.1016/j.fgb.2010.03.001

Cited by 34 publications

(41 citation statements)

References 61 publications

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“…Not too surprisingly, far fewer experimental demonstrations of organisms utilizing flavoHbs or Hbs for their protection against NO have been reported. Recent experiments support NOD functions for flavoHbs or Hbs expressed by Bacillus subtilis [212, 213], Staphylococcus aureus [214, 215], Aspergillus oryzae [112, 216], A. nidulans [113], A. fumigatus [114], Yersinia pestis [217], Vibrio fischeri [218], Pseudoalteromonas haloplanktis [219], Campylobacter jejuni [220, 221], the Japanese shrub Alnus firma [182], Sinorhizobium meliloti [183], Botrytis cinerea [222], and Synechococcus [138]. Expression of Mycobacterium leprae GlbO [223] and Synechocystis Syn Hb [133] alleviates NO toxicity in E. coli supporting a NOD function.…”

Section: Flavohbs and Hbs Detoxify Nomentioning

confidence: 99%

“…Stern and coworkers suggest that low constitutive levels of flavoHb protect V. cholerae from NO-dependent elimination [252]. In the case of the plant fungal necrotroph Botrytis cinerea , flavoHb-NOD was not found to be a virulence factor [222]. …”

Section: Nod Functions For Flavohbs and Hbs In Microbial Pathogenesismentioning

confidence: 99%

“…In Candida albicans , CTA4 a zinc-finger protein is required for induction of YHB1 transcription [245], and Cwt1p acts as a repressor of a nitrosative stress regulon that includes YHB1 [241]. NO upregulates flavoHb (NOD) expression by Aspergillus oryzae [216], the plant pathogen Botrytis cinerea [222] and other fungi [65] presumably via similar mechanisms. The full details of NO sensing and transcription activation remain to be elucidated.…”

Section: Regulation Of Globin Expression and Nod Functionmentioning

confidence: 99%

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Hemoglobin: A Nitric-Oxide Dioxygenase

Gardner

2012

Scientifica

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Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and when paired with native electron donors, function as NO dioxygenases (NODs). Indeed, the NOD function has emerged as a more common and ancient function than the well-known role in O2 transport-storage. Novel hemoglobins possessing a NOD function continue to be discovered in diverse life forms. Unique hemoglobin structures evolved, in part, for catalysis with different electron donors. The mechanism of NOD catalysis by representative single domain hemoglobins and multidomain flavohemoglobin occurs through a multistep mechanism involving O2 migration to the heme pocket, O2 binding-reduction, NO migration, radical-radical coupling, O-atom rearrangement, nitrate release, and heme iron re-reduction. Unraveling the physiological functions of multiple NODs with varying expression in organisms and the complexity of NO as both a poison and signaling molecule remain grand challenges for the NO field. NOD knockout organisms and cells expressing recombinant NODs are helping to advance our understanding of NO actions in microbial infection, plant senescence, cancer, mitochondrial function, iron metabolism, and tissue O2 homeostasis. NOD inhibitors are being pursued for therapeutic applications as antibiotics and antitumor agents. Transgenic NOD-expressing plants, fish, algae, and microbes are being developed for agriculture, aquaculture, and industry.

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Section: Flavohbs and Hbs Detoxify Nomentioning

confidence: 99%

Section: Nod Functions For Flavohbs and Hbs In Microbial Pathogenesismentioning

confidence: 99%

Section: Regulation Of Globin Expression and Nod Functionmentioning

confidence: 99%

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Hemoglobin: A Nitric-Oxide Dioxygenase

Gardner

2012

Scientifica

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“…NO at low concentrations protects Saccharomyces cerevisiae against heavy metal Cu 2+ toxicity, while high concentrations of NO have opposite effects (Chiang et al, 2000;Turrion-Gomez et al, 2010;Zhou et al, 2011). Also, low levels of NO show a cytoprotective effect on S. cerevisiae during heat shock stress and high hydrostatic pressure (Domitrovic et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Nitric oxide alleviates heat stress-induced oxidative damage in Pleurotus eryngii var. tuoliensis

WeiWei

Huang

Chen

et al. 2012

Fungal Genetics and Biology

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“…The human pathogenic fungus Cryptococcus neoformans counteracts cytotoxic nitrosative stress with the help of enzymes, such as flavohemoglobin denitrosylase and S-nitrosoglutathione reductase, which were shown to promote fungal virulence [21]. Similarly, a gene encoding flavohemoglobin ( BcFHG1 ) was shown to be essential for NO detoxification and provide protection against nitrosative conditions in the necrotrophic fungus B. cinerea [22]. Therefore, the relative sensitivity of fungal pathogens to oxidative and nitrosative stress depends on the effectiveness of their own ROS and RNS detoxification machinery.…”

Section: Introductionmentioning

confidence: 99%

Comparative Transcriptome Analysis of the Necrotrophic Fungus Ascochyta rabiei during Oxidative Stress: Insight for Fungal Survival in the Host Plant

et al. 2012

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Localized cell death, known as the hypersensitive response (HR), is an important defense mechanism for neutralizing phytopathogens. The hallmark of the HR is an oxidative burst produced by the host plant. We aimed to identify genes of the necrotrophic chickpea blight fungus Ascochyta rabiei that are involved in counteracting oxidative stress. A subtractive cDNA library was constructed after menadione treatment, which resulted in the isolation of 128 unigenes. A reverse northern blot was used to compare transcript profiles after H 2 O 2 , menadione and sodium nitroprusside treatments. A total of 70 unigenes were found to be upregulated by more than two-fold following menadione treatment at different time intervals. A large number of genes not previously associated with oxidative stress were identified, along with many stress-responsive genes. Differential expression patterns of several genes were validated by quantitative real-time PCR (qRT-PCR) and northern blotting. In planta qRT-PCR of several selected genes also showed differential expression patterns during infection and disease progression. These data shed light on the molecular responses of the phytopathogen A. rabiei to overcome oxidative and nitrosative stresses and advance the understanding of necrotrophic fungal pathogen survival mechanisms.

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The flavohemoglobin BCFHG1 is the main NO detoxification system and confers protection against nitrosative conditions but is not a virulence factor in the fungal necrotroph Botrytis cinerea

Cited by 34 publications

References 61 publications

Hemoglobin: A Nitric-Oxide Dioxygenase

Hemoglobin: A Nitric-Oxide Dioxygenase

Nitric oxide alleviates heat stress-induced oxidative damage in Pleurotus eryngii var. tuoliensis

Comparative Transcriptome Analysis of the Necrotrophic Fungus Ascochyta rabiei during Oxidative Stress: Insight for Fungal Survival in the Host Plant

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