Regulation of intracellular cyclic AMP levels in the white-rot fungus Phanerochaete chrysosporium during the onset of idiophasic metabolism

MacDonald, Malcolm J.; Ambler, R. P.; Broda, Paul

doi:10.1007/bf00447059

Cited by 15 publications

(9 citation statements)

References 18 publications

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“…Earlier studies showed that the transition from primary to secondary metabolism in filamentous fungi is positively correlated with a sharp increase in intracellular cAMP levels [50]. MacDonald and co-workers [51,52] showed an elevation in cAMP in cells grown under ligninolytic conditions (i.e. grown in low N medium) but not under nonligninolytic conditions (i.e.…”

Section: Regulation Of Lip Productionmentioning

confidence: 99%

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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Section: Regulation Of Lip Productionmentioning

confidence: 99%

Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium

Reddy¹

1994

FEMS Microbiology Reviews

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“…9,10) In 1992, Boominathan and Reddy indicated that atropine can inhibit ligninolytic enzyme production, and in this case, intracellular cAMP concentration did not increase in P. chrysosporium culture under low nitrogen conditions. They speculated that atropine inhibited adenylate cyclase, a key enzyme involved in cAMP synthesis, which might be required for ligninolytic enzyme production.…”

mentioning

confidence: 93%

Changes in the Gene Expression of the White Rot FungusPhanerochaete chrysosporiumDue to the Addition of Atropine

Minami

Suzuki

Shimizu

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…When cultivated under nitrogen-rich conditions, production of LIPs, MNPs, and other components ofthe lignin-degrading enzyme system is blocked. MacDonald and coworkers (4,5) reported an elevation in cAMP concentration in P. chrysosporium cultures grown under ligninolytic conditions in a low nitrogen medium but not in cultures grown under nonligninolytic conditions in a nitrogen-rich medium. Also, Mn2+ concentration in the growth medium was shown to be positively correlated to MNP production and negatively correlated to LIP production (for review, see ref.…”

mentioning

confidence: 99%

cAMP-mediated differential regulation of lignin peroxidase and manganese-dependent peroxidase production in the white-rot basidiomycete Phanerochaete chrysosporium.

Boominathan

Reddy

1992

Proc. Natl. Acad. Sci. U.S.A.

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Lignin peroxidases (LIPs) and manganesedependent peroxidases (MNPs) are major components of the -ignin-degrading enzyme system of Phanerochaete chrysosporium and typically appear during secondary metabolism. The involvement of cAMP in the regulation of production of LIPs and MNPs was investigated in this study. Production of LIPs and MNPs was preceded by a sharp rise in intracellular cAMP concentration. Addition of atropine, theophylline, or histamine to cultures resulted in a drop in intracellular cAMP concentration and a concomitant inhibition of production of LIPs only or of both LIPs and MNPs, depending on the concentration of the inhibitor added. These results were independently confirmed by fast protein liquid chromatographic proffles of the LIPs and MNPs in the extracellular fluid of the inhibitor-treated and untreated control cultures. LIP production was generally more sensitive to the inhibitors than MNP production. Northern blot analyses showed that the inhibitors affect the production of LIPs and MNPs at the level of transcription. Furthermore, LIP and MNP gene expression appears to be differentially regulated depending on the intracellular concentration of cAMP. These results show that cAMP plays a key role in the regulation of production of LIPs and MNPs in P. chrysosporium.The white-rot basidiomycete Phanerochaete chrysosporium has been the focus of intense worldwide research from the standpoint of lignin biodegradation and bioremediation of environmental pollutants (for review, see refs.

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Regulation of intracellular cyclic AMP levels in the white-rot fungus Phanerochaete chrysosporium during the onset of idiophasic metabolism

Cited by 15 publications

References 18 publications

Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium

Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium

Changes in the Gene Expression of the White Rot FungusPhanerochaete chrysosporiumDue to the Addition of Atropine

cAMP-mediated differential regulation of lignin peroxidase and manganese-dependent peroxidase production in the white-rot basidiomycete Phanerochaete chrysosporium.

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