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. 1996 Oct;62(10):3697–3703. doi: 10.1128/aem.62.10.3697-3703.1996

Expression of lip genes during growth in soil and oxidation of anthracene by Phanerochaete chrysosporium.

B W Bogan 1, B Schoenike 1, R T Lamar 1, D Cullen 1
PMCID: PMC168178  PMID: 8837425

Abstract

mRNA extraction from soil and quantitation by competitive reverse transcription-PCR were combined to study the expression of the 10 known lignin peroxidase (lip) genes in anthracene-transforming soil cultures of Phanerochaete chrysosporium. Levels of extractable lipA transcript and protein (LiP H8) were well correlated, although they were separated by a 2-day lag period. The patterns of transcript abundance over time in soil-grown P. chrysosporium varied among the nine lip mRNAs detected; comparison with lip gene expression under different liquid culture conditions suggested an early phase of carbon limitation for the cultures as a whole, which was followed by a transition to nitrogen starvation. Anthracene transformation occurred throughout the 25-day course of the experiment and, therefore, likely involves mechanisms distinct from those involved in oxidation of non-LiP substrate polycyclic aromatic hydrocarbons.

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Selected References

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  1. Bogan B. W., Lamar R. T. One-electron oxidation in the degradation of creosote polycyclic aromatic hydrocarbons by Phanerochaete chrysosporium. Appl Environ Microbiol. 1995 Jul;61(7):2631–2635. doi: 10.1128/aem.61.7.2631-2635.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bogan B. W., Schoenike B., Lamar R. T., Cullen D. Manganese peroxidase mRNA and enzyme activity levels during bioremediation of polycyclic aromatic hydrocarbon-contaminated soil with Phanerochaete chrysosporium. Appl Environ Microbiol. 1996 Jul;62(7):2381–2386. doi: 10.1128/aem.62.7.2381-2386.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boominathan K., D'Souza T. M., Naidu P. S., Dosoretz C., Reddy C. A. Temporal expression of the major lignin peroxidase genes of Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 Nov;59(11):3946–3950. doi: 10.1128/aem.59.11.3946-3950.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boominathan K., Reddy C. A. cAMP-mediated differential regulation of lignin peroxidase and manganese-dependent peroxidase production in the white-rot basidiomycete Phanerochaete chrysosporium. Proc Natl Acad Sci U S A. 1992 Jun 15;89(12):5586–5590. doi: 10.1073/pnas.89.12.5586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bumpus J. A. Biodegradation of polycyclic hydrocarbons by Phanerochaete chrysosporium. Appl Environ Microbiol. 1989 Jan;55(1):154–158. doi: 10.1128/aem.55.1.154-158.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Covert S. F., Vanden Wymelenberg A., Cullen D. Structure, organization, and transcription of a cellobiohydrolase gene cluster from Phanerochaete chrysosporium. Appl Environ Microbiol. 1992 Jul;58(7):2168–2175. doi: 10.1128/aem.58.7.2168-2175.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. D'Souza T. M., Dass S. B., Rasooly A., Reddy C. A. Electrophoretic karyotyping of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Mol Microbiol. 1993 May;8(5):803–807. doi: 10.1111/j.1365-2958.1993.tb01627.x. [DOI] [PubMed] [Google Scholar]
  8. Dass S. B., Reddy C. A. Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium. FEMS Microbiol Lett. 1990 Jun 1;57(3):221–224. doi: 10.1111/j.1574-6968.1990.tb04233.x. [DOI] [PubMed] [Google Scholar]
  9. Datta A., Bettermann A., Kirk T. K. Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay. Appl Environ Microbiol. 1991 May;57(5):1453–1460. doi: 10.1128/aem.57.5.1453-1460.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gaskell J., Dieperink E., Cullen D. Genomic organization of lignin peroxidase genes of Phanerochaete chrysosporium. Nucleic Acids Res. 1991 Feb 11;19(3):599–603. doi: 10.1093/nar/19.3.599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gaskell J., Stewart P., Kersten P. J., Covert S. F., Reiser J., Cullen D. Establishment of genetic linkage by allele-specific polymerase chain reaction: application to the lignin peroxidase gene family of Phanerochaete chrysosporium. Biotechnology (N Y) 1994 Dec;12(13):1372–1375. doi: 10.1038/nbt1294-1372. [DOI] [PubMed] [Google Scholar]
  12. Gaskell J., Van den Wymelenberg A., Cullen D. Structure, inheritance, and transcriptional effects of Pce1, an insertional element within Phanerochaete chrysosporium lignin peroxidase gene lipI. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7465–7469. doi: 10.1073/pnas.92.16.7465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Glumoff T., Harvey P. J., Molinari S., Goble M., Frank G., Palmer J. M., Smit J. D., Leisola M. S. Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes. Eur J Biochem. 1990 Feb 14;187(3):515–520. doi: 10.1111/j.1432-1033.1990.tb15333.x. [DOI] [PubMed] [Google Scholar]
  14. Haemmerli S. D., Leisola M. S., Sanglard D., Fiechter A. Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase. J Biol Chem. 1986 May 25;261(15):6900–6903. [PubMed] [Google Scholar]
  15. Hammel K. E., Gai W. Z., Green B., Moen M. A. Oxidative degradation of phenanthrene by the ligninolytic fungus Phanerochaete chrysosporium. Appl Environ Microbiol. 1992 Jun;58(6):1832–1838. doi: 10.1128/aem.58.6.1832-1838.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hammel K. E., Green B., Gai W. Z. Ring fission of anthracene by a eukaryote. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10605–10608. doi: 10.1073/pnas.88.23.10605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hammel K. E., Kalyanaraman B., Kirk T. K. Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase. J Biol Chem. 1986 Dec 25;261(36):16948–16952. [PubMed] [Google Scholar]
  18. Holzbaur E. L., Andrawis A., Tien M. Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium. Biochem Biophys Res Commun. 1988 Sep 15;155(2):626–633. doi: 10.1016/s0006-291x(88)80541-2. [DOI] [PubMed] [Google Scholar]
  19. Johnston C. G., Aust S. D. Detection of Phanerochaete chrysosporium in soil by PCR and restriction enzyme analysis. Appl Environ Microbiol. 1994 Jul;60(7):2350–2354. doi: 10.1128/aem.60.7.2350-2354.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kersten P. J., Cullen D. Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7411–7413. doi: 10.1073/pnas.90.15.7411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lamar R. T., Larsen M. J., Kirk T. K. Sensitivity to and Degradation of Pentachlorophenol by Phanerochaete spp. Appl Environ Microbiol. 1990 Nov;56(11):3519–3526. doi: 10.1128/aem.56.11.3519-3526.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Lamar R. T., Schoenike B., Vanden Wymelenberg A., Stewart P., Dietrich D. M., Cullen D. Quantitation of fungal mRNAs in complex substrates by reverse transcription PCR and its application to Phanerochaete chrysosporium-colonized soil. Appl Environ Microbiol. 1995 Jun;61(6):2122–2126. doi: 10.1128/aem.61.6.2122-2126.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Millis C. D., Cai D. Y., Stankovich M. T., Tien M. Oxidation-reduction potentials and ionization states of extracellular peroxidases from the lignin-degrading fungus Phanerochaete chrysosporium. Biochemistry. 1989 Oct 17;28(21):8484–8489. doi: 10.1021/bi00447a032. [DOI] [PubMed] [Google Scholar]
  24. Moen M. A., Hammel K. E. Lipid Peroxidation by the Manganese Peroxidase of Phanerochaete chrysosporium Is the Basis for Phenanthrene Oxidation by the Intact Fungus. Appl Environ Microbiol. 1994 Jun;60(6):1956–1961. doi: 10.1128/aem.60.6.1956-1961.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Moukha S. M., Wösten H. A., Mylius E. J., Asther M., Wessels J. G. Spatial and temporal accumulation of mRNAs encoding two common lignin peroxidases in Phanerochaete chrysosporium. J Bacteriol. 1993 Jun;175(11):3672–3678. doi: 10.1128/jb.175.11.3672-3678.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Orth A. B., Royse D. J., Tien M. Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi. Appl Environ Microbiol. 1993 Dec;59(12):4017–4023. doi: 10.1128/aem.59.12.4017-4023.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Pannetier C., Delassus S., Darche S., Saucier C., Kourilsky P. Quantitative titration of nucleic acids by enzymatic amplification reactions run to saturation. Nucleic Acids Res. 1993 Feb 11;21(3):577–583. doi: 10.1093/nar/21.3.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Raeder U., Thompson W., Broda P. RFLP-based genetic map of Phanerochaete chrysosporium ME446: lignin peroxidase genes occur in clusters. Mol Microbiol. 1989 Jul;3(7):911–918. doi: 10.1111/j.1365-2958.1989.tb00240.x. [DOI] [PubMed] [Google Scholar]
  29. Reiser J., Walther I. S., Fraefel C., Fiechter A. Methods to investigate the expression of lignin peroxidase genes by the white rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 Sep;59(9):2897–2903. doi: 10.1128/aem.59.9.2897-2903.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Ritch T. G., Jr, Gold M. H. Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporium. Gene. 1992 Sep 1;118(1):73–80. doi: 10.1016/0378-1119(92)90250-s. [DOI] [PubMed] [Google Scholar]
  31. Selvaratnam S., Schoedel B. A., McFarland B. L., Kulpa C. F. Application of reverse transcriptase PCR for monitoring expression of the catabolic dmpN gene in a phenol-degrading sequencing batch reactor. Appl Environ Microbiol. 1995 Nov;61(11):3981–3985. doi: 10.1128/aem.61.11.3981-3985.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Sinclair R., Copeland B., Yamazaki I., Powers L. X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10. Biochemistry. 1995 Oct 10;34(40):13176–13182. doi: 10.1021/bi00040a032. [DOI] [PubMed] [Google Scholar]
  33. Stewart P., Kersten P., Vanden Wymelenberg A., Gaskell J., Cullen D. Lignin peroxidase gene family of Phanerochaete chrysosporium: complex regulation by carbon and nitrogen limitation and identification of a second dimorphic chromosome. J Bacteriol. 1992 Aug;174(15):5036–5042. doi: 10.1128/jb.174.15.5036-5042.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Urzúa U., Fernando Larrondo L., Lobos S., Larraín J., Vicuña R. Oxidation reactions catalyzed by manganese peroxidase isoenzymes from Ceriporiopsis subvermispora. FEBS Lett. 1995 Sep 4;371(2):132–136. doi: 10.1016/0014-5793(95)00874-9. [DOI] [PubMed] [Google Scholar]
  35. Vares T., Kalsi M., Hatakka A. Lignin Peroxidases, Manganese Peroxidases, and Other Ligninolytic Enzymes Produced by Phlebia radiata during Solid-State Fermentation of Wheat Straw. Appl Environ Microbiol. 1995 Oct;61(10):3515–3520. doi: 10.1128/aem.61.10.3515-3520.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Vazquez-Duhalt R., Westlake D. W., Fedorak P. M. Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvents. Appl Environ Microbiol. 1994 Feb;60(2):459–466. doi: 10.1128/aem.60.2.459-466.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]

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