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Transcript and activity levels of different Pleurotus ostreatus peroxidases are differentially affected by Mn 2+
Year:
2001
Source of publication :
Environmental Microbiology
Authors :
כהן, רוני
;
.
Volume :
3
Co-Authors:
Cohen, R., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel
Hadar, Y., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel, Department of Plant Pathology and Microbiology, Israel
Yarden, O., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel
Facilitators :
From page:
312
To page:
322
(
Total pages:
11
)
Abstract:
The white-rot fungus Pleurotus ostreatus produces both manganese-dependent peroxidase (MnP) and versatile peroxidase (VP) in non-manganese-amended peptone medium (PM). We studied the effect of Mn 2+ supplementation on MnPs and VPs in P. ostreatus by analysing the enzymatic and transcript abundance profiles of the peroxidases, as well as the lignin mineralization rate. The fungus was grown in PM under solid-state conditions using perlite as an inert solid support. Mn 2+ amendment resulted in a 1.7-fold increase in [ 14C]-lignin mineralization relative to unamended medium. Anion-exchange chromatography was used to resolve the fungal peroxidase's enzymatic activity profile. Five peaks (P1-P5) of VP and one peak (P6) of MnP activity were detected in unamended medium. In Mn 2+-amended medium, a reduction in the activity of the VPs was observed. On the other hand, a sharp increase in the MnP activity level of peak P6 was detected. The P6 isoenzyme was purified and showed manganese-dependent peroxidation of phenolic substrates. Internal sequence analysis of the purified enzyme revealed 100% identity with the deduced amino acid sequence of P. ostreatus MnP3 (GenBank AB016519). The effect of Mn 2+ on the relative abundance of gene transcripts of three VPs and one MnP from P. ostreatus was monitored using reverse transcription-polymerase chain reaction (RT-PCR) with oligonucleotide primer sets synthesized on the basis of non-conserved sequences of the different peroxidases. The reduction in VP gene transcript abundance and the increase in mnp3 transcript level were collinear with the changes observed in the enzyme activity profiles. These results indicate that the activity of peroxidases is regulated at the transcriptional level. We suggest that the expression of MnP and VP may be differentially regulated by the presence of Mn 2+.
Note:
Related Files :
Eukaryota
fungi
Gene Expression Regulation, Fungal
Molecular Sequence Data
Pleurotus ostreatus
RNA, Messenger
עוד תגיות
תוכן קשור
More details
DOI :
10.1046/j.1462-2920.2001.00197.x
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
27317
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:29
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Scientific Publication
Transcript and activity levels of different Pleurotus ostreatus peroxidases are differentially affected by Mn 2+
3
Cohen, R., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel
Hadar, Y., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel, Department of Plant Pathology and Microbiology, Israel
Yarden, O., Department of Plant Pathology and Microbiology, Otto Warburg Center for Biotechnology in Agriculture, Hebrew University of Jerusalem, PO Box 12, Rehovot 76100, Israel
Transcript and activity levels of different Pleurotus ostreatus peroxidases are differentially affected by Mn 2+
The white-rot fungus Pleurotus ostreatus produces both manganese-dependent peroxidase (MnP) and versatile peroxidase (VP) in non-manganese-amended peptone medium (PM). We studied the effect of Mn 2+ supplementation on MnPs and VPs in P. ostreatus by analysing the enzymatic and transcript abundance profiles of the peroxidases, as well as the lignin mineralization rate. The fungus was grown in PM under solid-state conditions using perlite as an inert solid support. Mn 2+ amendment resulted in a 1.7-fold increase in [ 14C]-lignin mineralization relative to unamended medium. Anion-exchange chromatography was used to resolve the fungal peroxidase's enzymatic activity profile. Five peaks (P1-P5) of VP and one peak (P6) of MnP activity were detected in unamended medium. In Mn 2+-amended medium, a reduction in the activity of the VPs was observed. On the other hand, a sharp increase in the MnP activity level of peak P6 was detected. The P6 isoenzyme was purified and showed manganese-dependent peroxidation of phenolic substrates. Internal sequence analysis of the purified enzyme revealed 100% identity with the deduced amino acid sequence of P. ostreatus MnP3 (GenBank AB016519). The effect of Mn 2+ on the relative abundance of gene transcripts of three VPs and one MnP from P. ostreatus was monitored using reverse transcription-polymerase chain reaction (RT-PCR) with oligonucleotide primer sets synthesized on the basis of non-conserved sequences of the different peroxidases. The reduction in VP gene transcript abundance and the increase in mnp3 transcript level were collinear with the changes observed in the enzyme activity profiles. These results indicate that the activity of peroxidases is regulated at the transcriptional level. We suggest that the expression of MnP and VP may be differentially regulated by the presence of Mn 2+.
Scientific Publication
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