Manganese peroxidase gene transcription in Phanerochaete chrysosporium: activation by manganese.
Identifieur interne : 000F12 ( Main/Exploration ); précédent : 000F11; suivant : 000F13Manganese peroxidase gene transcription in Phanerochaete chrysosporium: activation by manganese.
Auteurs : J A Brown ; M. Alic ; M H GoldSource :
- Journal of bacteriology [ 0021-9193 ] ; 1991.
Descripteurs français
- KwdFr :
- Activation enzymatique (effets des médicaments et des substances chimiques), Basidiomycota (enzymologie), Basidiomycota (génétique), Données de séquences moléculaires (MeSH), Manganèse (pharmacologie), Peroxidases (génétique), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Séquence nucléotidique (MeSH), Transcription génétique (MeSH).
- MESH :
- effets des médicaments et des substances chimiques : Activation enzymatique, Régulation de l'expression des gènes fongiques.
- enzymologie : Basidiomycota.
- génétique : Basidiomycota, Peroxidases.
- pharmacologie : Manganèse.
- Données de séquences moléculaires, Séquence nucléotidique, Transcription génétique.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Peroxidases.
- chemical , pharmacology : Manganese.
- drug effects : Enzyme Activation, Gene Expression Regulation, Fungal.
- enzymology : Basidiomycota.
- genetics : Basidiomycota.
- Base Sequence, Molecular Sequence Data, Transcription, Genetic.
Abstract
The expression of manganese peroxidase in nitrogen-limited cultures of Phanerochaete chrysosporium is dependent on Mn, and initial work suggested that Mn regulates transcription of the mnp gene. In this study, using Northern (RNA) blot analysis of kinetic, dose-response, and inhibitor experiments, we demonstrate unequivocally that Mn regulates mnp gene transcription. The amount of mnp mRNA in cells of 4-day-old nitrogen-limited cultures is a direct function of the concentration of Mn in the culture medium up to a maximum of 180 microM. Addition of Mn to nitrogen-limited Mn-deficient secondary metabolic (4-, 5-, and 6-day-old) cultures results in the appearance of mnp mRNA within 40 min. The appearance of this message is completely inhibited by the RNA synthesis inhibitor dactinomycin but not by the protein synthesis inhibitor cycloheximide. Furthermore, the amount of mnp mRNA produced is a direct function of the concentration of added Mn. In contrast, addition of Mn to low-nitrogen Mn-deficient 2- or 3-day-old cultures does not result in the appearance of mnp mRNA. Manganese peroxidase protein is detected by specific immunoprecipitation of the in vitro translation products of poly(A) RNA isolated from Mn-supplemented (but not from Mn-deficient) cells. All of these results demonstrate that Mn, the substrate for the enzyme, regulates mnp gene transcription via a growth-stage-specific and concentration-dependent mechanism.
DOI: 10.1128/jb.173.13.4101-4106.1991
PubMed: 2061289
PubMed Central: PMC208059
Affiliations:
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Le document en format XML
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<term>Enzyme Activation (drug effects)</term>
<term>Gene Expression Regulation, Fungal (drug effects)</term>
<term>Manganese (pharmacology)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Peroxidases (genetics)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (effets des médicaments et des substances chimiques)</term>
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<term>Basidiomycota (génétique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Manganèse (pharmacologie)</term>
<term>Peroxidases (génétique)</term>
<term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Transcription génétique (MeSH)</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Activation</term>
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<front><div type="abstract" xml:lang="en">The expression of manganese peroxidase in nitrogen-limited cultures of Phanerochaete chrysosporium is dependent on Mn, and initial work suggested that Mn regulates transcription of the mnp gene. In this study, using Northern (RNA) blot analysis of kinetic, dose-response, and inhibitor experiments, we demonstrate unequivocally that Mn regulates mnp gene transcription. The amount of mnp mRNA in cells of 4-day-old nitrogen-limited cultures is a direct function of the concentration of Mn in the culture medium up to a maximum of 180 microM. Addition of Mn to nitrogen-limited Mn-deficient secondary metabolic (4-, 5-, and 6-day-old) cultures results in the appearance of mnp mRNA within 40 min. The appearance of this message is completely inhibited by the RNA synthesis inhibitor dactinomycin but not by the protein synthesis inhibitor cycloheximide. Furthermore, the amount of mnp mRNA produced is a direct function of the concentration of added Mn. In contrast, addition of Mn to low-nitrogen Mn-deficient 2- or 3-day-old cultures does not result in the appearance of mnp mRNA. Manganese peroxidase protein is detected by specific immunoprecipitation of the in vitro translation products of poly(A) RNA isolated from Mn-supplemented (but not from Mn-deficient) cells. All of these results demonstrate that Mn, the substrate for the enzyme, regulates mnp gene transcription via a growth-stage-specific and concentration-dependent mechanism.</div>
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<Abstract><AbstractText>The expression of manganese peroxidase in nitrogen-limited cultures of Phanerochaete chrysosporium is dependent on Mn, and initial work suggested that Mn regulates transcription of the mnp gene. In this study, using Northern (RNA) blot analysis of kinetic, dose-response, and inhibitor experiments, we demonstrate unequivocally that Mn regulates mnp gene transcription. The amount of mnp mRNA in cells of 4-day-old nitrogen-limited cultures is a direct function of the concentration of Mn in the culture medium up to a maximum of 180 microM. Addition of Mn to nitrogen-limited Mn-deficient secondary metabolic (4-, 5-, and 6-day-old) cultures results in the appearance of mnp mRNA within 40 min. The appearance of this message is completely inhibited by the RNA synthesis inhibitor dactinomycin but not by the protein synthesis inhibitor cycloheximide. Furthermore, the amount of mnp mRNA produced is a direct function of the concentration of added Mn. In contrast, addition of Mn to low-nitrogen Mn-deficient 2- or 3-day-old cultures does not result in the appearance of mnp mRNA. Manganese peroxidase protein is detected by specific immunoprecipitation of the in vitro translation products of poly(A) RNA isolated from Mn-supplemented (but not from Mn-deficient) cells. All of these results demonstrate that Mn, the substrate for the enzyme, regulates mnp gene transcription via a growth-stage-specific and concentration-dependent mechanism.</AbstractText>
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