Nitrogen regulation of lignin peroxidase and manganese-dependent peroxidase production is independent of carbon and manganese regulation in Phanerochaete chrysosporium

Woude, Marjan W. van der; Boominathan, K.; Reddy, C. A.

doi:10.1007/bf00258138

Cited by 30 publications

(18 citation statements)

References 7 publications

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“…In parallel, a decline in ligninolytic and cellulolytic enzyme activities has been observed in the forest floor [19]. Under laboratory conditions, high inorganic nitrogen concentrations can repress transcription of lignocellulolytic genes [53], [54]. This raises the question: might anthropogenic nitrogen deposition elicit a similar effect?…”

Section: Resultsmentioning

confidence: 99%

Fungi Unearthed: Transcripts Encoding Lignocellulolytic and Chitinolytic Enzymes in Forest Soil

Kellner

Vandenbol

2010

PLoS ONE

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BackgroundFungi are the main organisms responsible for the degradation of biopolymers such as lignin, cellulose, hemicellulose, and chitin in forest ecosystems. Soil surveys largely target fungal diversity, paying less attention to fungal activity.Methodology/Principal FindingsHere we have focused on the organic horizon of a hardwood forest dominated by sugar maple that spreads widely across Eastern North America. The sampling site included three plots receiving normal atmospheric nitrogen deposition and three that received an extra 3 g nitrogen m−2 y−1 in form of sodium nitrate pellets since 1994, which led to increased accumulation of organic matter in the soil. Our aim was to assess, in samples taken from all six plots, transcript-level expression of fungal genes encoding lignocellulolytic and chitinolytic enzymes. For this we collected RNA from the forest soil, reverse-transcribed it, and amplified cDNAs of interest, using both published primer pairs as well as 23 newly developed ones. We thus detected transcript-level expression of 234 genes putatively encoding 26 different groups of fungal enzymes, notably major ligninolytic and diverse aromatic-oxidizing enzymes, various cellulose- and hemicellulose-degrading glycoside hydrolases and carbohydrate esterases, enzymes involved in chitin breakdown, N-acetylglucosamine metabolism, and cell wall degradation. Among the genes identified, 125 are homologous to known ascomycete genes and 105 to basidiomycete genes. Transcripts corresponding to all 26 enzyme groups were detected in both control and nitrogen-supplemented plots.Conclusions/SignificanceMany of these enzyme groups are known to be important in soil turnover processes, but the contribution of some is probably underestimated. Our data highlight the importance of ascomycetes, as well as basidiomycetes, in important biogeochemical cycles. In the nitrogen-supplemented plots, we have detected no transcript-level gap likely to explain the observed increased carbon storage, which is more likely due to community changes and perhaps transcriptional and/or post-transcriptional down-regulation of relevant genes.

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Section: Resultsmentioning

confidence: 99%

Fungi Unearthed: Transcripts Encoding Lignocellulolytic and Chitinolytic Enzymes in Forest Soil

Kellner

Vandenbol

2010

PLoS ONE

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“…1) showed that nitrogen regulation of LiP and MnP production is independent of carbon regulation as evidenced by the fact that der8-5 141 produces both LiPs and MnPs (as expected) in excess N medium; however, in excess carbon medium the LiP and MnP production by this mutant is completely suppressed. WT produces neither LiPs nor MnPs in these two media because LiP and MnP production by it is known to be repressed in the presence of excess N or C [47]. The results further showed that Mn(II) regulation of LiP and MnP production is independent of nitrogen regulation in that LiP and MnP production by der8-5 is subject to Mn(II) regulation regardless of the fact whether it is grown in low N medium or in high N medium.…”

Section: Regulation Of Lip Productionmentioning

confidence: 85%

Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium

Reddy¹

1994

FEMS Microbiology Reviews

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The white-rot basidiomycete Phanerochaete chrysosporium produces lignin peroxidases (LiPs), a family of extracellular glycosylated heme proteins, as major components of its lignin-degrading system. Up to 15 LiP isozymes, ranging in M(r) values from 38,000 to 43,000, are produced depending on culture conditions and strains employed. Manganese-dependent peroxidases (MnPs) are a second family of extracellular heme proteins produced by P. chrysosporium that are also believed to be important in lignin degradation by this organism. LiP and MnP production is seen during secondary metabolism and is completely suppressed under conditions of excess nitrogen and carbon. Excess Mn(II) in the medium, on the other hand, suppresses LiP production but enhances MnP production. Nitrogen regulation of LiP and MnP production is independent of carbon and Mn(II) regulation. LiP activity is also affected by idiophasic extracellular proteases. Intracellular cAMP levels appear to be important in regulating the production of LiPs and MnPs, although LiP production is affected more than MnP production. Studies on the sequencing and characterization of lip cDNAs and genes of P. chrysosporium have shown that the major LiP isozymes are each encoded by a separate gene. Each lip gene encodes a mature protein that is 343-344 amino acids long, contains 1 putative N-glycosylation site, a number of putative O-glycosylation sites, and is preceded by a 27-28-amino acid leader peptide ending in a Lys-Arg cleavage site. The coding region of each lip gene is interrupted by 8-9 introns (50-63 bp), and the positions of the last two introns appear to be highly conserved. There are substantial differences in the temporal transcription patterns of the major lip genes. The sequence data suggest the presence of three lip gene subfamilies. The genomic DNA of P. chrysosporium strain BKMF-1767 was resolved into 10 chromosomes (genome size of 29 Mb), and that of strain ME-446 into 11 chromosomes (genome size of 32 Mb). The lip genes have been localized to five chromosomes in BKMF-1767 and to four chromosomes in ME-446. DNA transformation studies have reported both integrative and non-integrative transformation in P. chrysosporium.

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“…However, some of the research results have proven to be controversial; the discrepancy is based on enzymes actuation, which is attributed to their selective specificity concerning turn of the substrate (Lee 2007). Several authors agree that nitrogen-limitation increases ligninolytic activities through stimulation of LiP and MnP secretion (Van der Woude et al 1993;Gao et al 2008Gao et al , 2010. On the other hand, other results have shown that strains pre-grown on nitrogen-rich medium also exhibit enhanced decolourization rate (Adosinda et al 2001(Adosinda et al , 2002.…”

Section: Introductionmentioning

confidence: 99%

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

et al. 2014

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Enzyme production by immobilized Phanerochaete chrysosporium was evaluated in airlift bioreactor and agitated cultures. Free mycelium and immobilized mycelium on alginate beads were tested in the decolourization of 50 and 500 mg/L of Remazol Brilliant Blue R. Dye concentration did not inhibit the fungi development in all tests. In addition, high decolourization percentage of dye was found with free mycelium (99%) in agitated flasks and with immobilized mycelium in airlift (98%). However, decolourization period by immobilized mycelium (120 h) was greater than that by the free mycelium (14 h). Important manganese peroxidase, lignine peroxidase and laccase activities were identified in decolourization process. Manganese peroxidase appeared to be promoted by high dye concentrations during the treatment with immobilized mycelium, but this enzyme was not detected with free mycelium in airlift. Bioreactor prompted also laccase and lignine peroxidase actions in both tests; free mycelium registered a maximum laccase action of 31.569 × 10 3 U/L in 70 h, whereas immobilized mycelium registered 1.680 × 10 3 U/L in 170 h, while lignine peroxidase secretion by free P. chrysosporium was higher (1.300 × 10 3 U/L) than immobilized mycelium (1.250 × 10 3 U/L). Maximum laccase activity coincided with the maximum percentage of decolourization, however, high peroxidase activity was identified from the start of dye treatment.

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Nitrogen regulation of lignin peroxidase and manganese-dependent peroxidase production is independent of carbon and manganese regulation in Phanerochaete chrysosporium

Cited by 30 publications

References 7 publications

Fungi Unearthed: Transcripts Encoding Lignocellulolytic and Chitinolytic Enzymes in Forest Soil

Fungi Unearthed: Transcripts Encoding Lignocellulolytic and Chitinolytic Enzymes in Forest Soil

Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

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