Regulation of glutamine synthetase activity by transcriptional and posttranslational modifications negatively influences ganoderic acid biosynthesis in <i>Ganoderma lucidum</i>

Zhu, Jing; Song, Seok-Bo; Sun, Zehua; Lian, Li; Shi, Liang; Ren, Ang; Zhao, Mingwen

doi:10.1111/1462-2920.15400

Cited by 12 publications

(15 citation statements)

References 59 publications

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“…In plants, bacteria, and animals it is widely accepted that the GlnS is regulated at the level of transcription, posttranscription, translation, and post translation. Though little is known about the regulatory mechanism of GlnS activity in fungi [ 43 ], one of those mechanisms might be the reason why we could not detect GlnS activity in P. sedebokerense . We thus searched for the GlnS gene in the draft genome (unpublished) of our P. sedebokerense strain.…”

Section: Resultsmentioning

confidence: 89%

“…We failed to detect fungal GlnS enzyme activity, although we used different assays. Little is known about the regulatory mechanism of GlnS activity in fungi; however, it was recently shown that transcriptional and posttranslational modifications are involved in the regulation of GlnS activity in the fungus Ganoderma lucidum [ 43 ]. We assume that in P. sedebokerense, GlnS is active during a specific growth stage which we could not identify yet.…”

Section: Discussionmentioning

confidence: 99%

“…Biosynthesis inhibitors of other amino acids have proven to be effective in controlling P. sedebokerense infection, i.e., methionine biosynthesis inhibitors [ 17 ]. GlnS plays a central role in the nitrogen metabolism of fungi [ 43 , 44 ], because it converts inorganic nitrogen (in the form of ammonia) to organic nitrogen in the form of glutamine [ 27 , 28 , 45 ], from which all amino acids are produced; consequently, GlnS should be a major target to control the disease to H. lacustris . We found that the GlnS present in the genome of P. sedebokerense is a GlnS type III.…”

Section: Discussionmentioning

confidence: 99%

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Paraphysoderma sedebokerense GlnS III Is Essential for the Infection of Its Host Haematococcus lacustris

Alors

Amses

James

et al. 2022

JoF

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Glutamine synthetase (GlnS) is a key enzyme in nitrogen metabolism. We investigated the effect of the GlnS inhibitor glufosinate on the infection of H. lacustris by the blastocladialean fungus P. sedebokerense, assuming that interfering with the host nitrogen metabolism will affect the success of the parasite. Complete inhibition of infection, which could be bypassed by the GlnS product glutamine, was observed at millimolar concentrations of glufosinate. However, this effect of glufosinate was attributed to its direct interaction with the blastoclad and not the host, which results in development and growth inhibition of the blastoclad. In our P. sedebokerense draft genome, we found that the sequence of GlnS is related to another fungal GlnS, type III, found in many poor known phyla of fungi, including Blastocladiomycota and Chytridiomycota, and absent in the main subkingdom of fungi, the Dikarya. We further tested the ability of the blastoclad to utilize nitrate and ammonia as inorganic nitrogen sources and glutamine for growth. We found that P. sedebokerense equally use ammonia and glutamine and use also nitrate, but with less efficiency. Altogether, our results show that GlnS type III is mandatory for the development and growth of P. sedebokerense and could be an efficient target to develop strategies for the control of the fungal parasite of H. lacustris.

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Section: Resultsmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Paraphysoderma sedebokerense GlnS III Is Essential for the Infection of Its Host Haematococcus lacustris

Alors

Amses

James

et al. 2022

JoF

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“…Total RNA was isolated with 1 ml of RNAiso Plus (TaKaRa) from 50 mg fresh mycelia and subsequently reverse transcribed to cDNA with a PrimeScript RT reagent kit (TaKaRa). Gene expression analysis was performed by qRT‐PCR according to a previous method (Zhu et al, 2021). The expression levels of the spds1 , spds2 , pao , odc and Glmyb genes under different heat stress times were analysed with 18S rRNA used as an internal standard gene (primers listed in Table 1).…”

Section: Methodsmentioning

confidence: 99%

Phospholipase D and phosphatidic acid mediate regulation in the biosynthesis of spermidine and ganoderic acids by activating GlMyb in Ganoderma lucidum under heat stress

Han

Wang

Shi

et al. 2022

Environmental Microbiology

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Polyamines are essential for all kinds of organisms and take part in the regulation of multiple biological processes. Our previous study revealed that heat stress promoted the conversion of putrescine to spermidine and subsequently promoted the accumulation of ganoderic acids (GAs). However, how heat stress affects polyamine homeostasis remains unclear. To explore the underlying mechanism by which heat stress promoted spermidine biosynthesis, we assessed the effects of signalling molecules that respond to heat stress on spermidine biosynthesis. Our data suggested that heat stress‐induced spermidine biosynthesis and GAs accumulation via a phospholipase D (PLD)‐mediated phosphatidic acid (PA) signal. Further research revealed that the transcription factor GlMyb promoted spermidine biosynthesis via regulating spermidine synthase genes (spds1 and spds2) expression by directly bonding to their promoters and it responded to heat stress and PA signal. In summary, heat stress activated GlMyb by PLD‐mediated PA signalling and subsequently induced the expression of spds1 and spds2 to promote the biosynthesis of spermidine and the accumulation of GAs. Our findings firstly reveal a detailed mechanism by which heat signalling regulates polyamine homeostasis by PLD‐mediated PA signal in fungi and provide a greater understanding of how organisms alter polyamine levels in response to environmental changes.

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“…These enzymes enable the initial N incorporation to the amino acids Gln, Glu, Asn, and Asp assimilation, but also GS has been identified as targets of nitration (Lozano-Juste et al, 2011). GS enzymes from mammals and fungi seem to be nitrated and inactivated, thus affecting the metabolism of Glu and ammonia in liver (Frieg et al, 2021) and the secondary metabolism in fungi (Zhu et al, 2021), respectively. Plant GDH seem to be involved mainly in Glu oxidation to supply cells with carbon skeletons under carbon limiting conditions (Robinson et al, 1991).…”

Section: Nitration Of the Enzymes Of Nitrate Assimilation And No Bios...mentioning

confidence: 99%

Protein Tyrosine Nitration in Plant Nitric Oxide Signaling

León

2022

Front. Plant Sci.

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Nitric oxide (NO), which is ubiquitously present in living organisms, regulates many developmental and stress-activated processes in plants. Regulatory effects exerted by NO lies mostly in its chemical reactivity as a free radical. Proteins are main targets of NO action as several amino acids can undergo NO-related post-translational modifications (PTMs) that include mainly S-nitrosylation of cysteine, and nitration of tyrosine and tryptophan. This review is focused on the role of protein tyrosine nitration on NO signaling, making emphasis on the production of NO and peroxynitrite, which is the main physiological nitrating agent; the main metabolic and signaling pathways targeted by protein nitration; and the past, present, and future of methodological and strategic approaches to study this PTM. Available information on identification of nitrated plant proteins, the corresponding nitration sites, and the functional effects on the modified proteins will be summarized. However, due to the low proportion of in vivo nitrated peptides and their inherent instability, the identification of nitration sites by proteomic analyses is a difficult task. Artificial nitration procedures are likely not the best strategy for nitration site identification due to the lack of specificity. An alternative to get artificial site-specific nitration comes from the application of genetic code expansion technologies based on the use of orthogonal aminoacyl-tRNA synthetase/tRNA pairs engineered for specific noncanonical amino acids. This strategy permits the programmable site-specific installation of genetically encoded 3-nitrotyrosine sites in proteins expressed in Escherichia coli, thus allowing the study of the effects of specific site nitration on protein structure and function.

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Regulation of glutamine synthetase activity by transcriptional and posttranslational modifications negatively influences ganoderic acid biosynthesis in Ganoderma lucidum

Cited by 12 publications

References 59 publications

Paraphysoderma sedebokerense GlnS III Is Essential for the Infection of Its Host Haematococcus lacustris

Paraphysoderma sedebokerense GlnS III Is Essential for the Infection of Its Host Haematococcus lacustris

Phospholipase D and phosphatidic acid mediate regulation in the biosynthesis of spermidine and ganoderic acids by activating GlMyb in Ganoderma lucidum under heat stress

Protein Tyrosine Nitration in Plant Nitric Oxide Signaling

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