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. 1995 Aug 1;92(16):7465–7469. doi: 10.1073/pnas.92.16.7465

Structure, inheritance, and transcriptional effects of Pce1, an insertional element within Phanerochaete chrysosporium lignin peroxidase gene lipI.

J Gaskell 1, A Van den Wymelenberg 1, D Cullen 1
PMCID: PMC41360  PMID: 7638214

Abstract

A 1747-bp insertion within a lignin peroxidase allele of Phanerochaete chrysosporium BKM-F-1767 is described. Pce1, the element, lies immediately adjacent to the fourth intron of lip12. Southern blots reveal the presence of Pce1-homologous sequences in other P. chrysosporium strains. Transposon-like features include inverted terminal repeats and a dinucleotide (TA) target duplication. Atypical of transposons, Pce1 is present at very low copy numbers (one to five copies), and conserved transposase motifs are lacking. The mutation transcriptionally inactivates lip12 and is inherited in a 1:1 Mendelian fashion among haploid progeny. Thus, Pce1 is a transposon-like element that may play a significant role in generating ligninolytic variation in certain P. chrysosporium strains.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alic M., Letzring C., Gold M. H. Mating System and Basidiospore Formation in the Lignin-Degrading Basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol. 1987 Jul;53(7):1464–1469. doi: 10.1128/aem.53.7.1464-1469.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brown J. A., Glenn J. K., Gold M. H. Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium. J Bacteriol. 1990 Jun;172(6):3125–3130. doi: 10.1128/jb.172.6.3125-3130.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Daboussi M. J., Langin T., Brygoo Y. Fot1, a new family of fungal transposable elements. Mol Gen Genet. 1992 Mar;232(1):12–16. doi: 10.1007/BF00299131. [DOI] [PubMed] [Google Scholar]
  4. Doak T. G., Doerder F. P., Jahn C. L., Herrick G. A proposed superfamily of transposase genes: transposon-like elements in ciliated protozoa and a common "D35E" motif. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):942–946. doi: 10.1073/pnas.91.3.942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dobinson K. F., Hamer J. E. The ebb and flow of a fungal genome. Trends Microbiol. 1993 Dec;1(9):348–352. doi: 10.1016/0966-842x(93)90076-4. [DOI] [PubMed] [Google Scholar]
  6. Dobinson K. F., Harris R. E., Hamer J. E. Grasshopper, a long terminal repeat (LTR) retroelement in the phytopathogenic fungus Magnaporthe grisea. Mol Plant Microbe Interact. 1993 Jan-Feb;6(1):114–126. doi: 10.1094/mpmi-6-114. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. Gaskell J., Vanden Wymelenberg A., Stewart P., Cullen D. Method to identify specific alleles of a Phanerochaete chrysosporium gene encoding lignin peroxidase. Appl Environ Microbiol. 1992 Apr;58(4):1379–1381. doi: 10.1128/aem.58.4.1379-1381.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Gold M. H., Alic M. Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Microbiol Rev. 1993 Sep;57(3):605–622. doi: 10.1128/mr.57.3.605-622.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Kachroo P., Leong S. A., Chattoo B. B. Pot2, an inverted repeat transposon from the rice blast fungus Magnaporthe grisea. Mol Gen Genet. 1994 Nov 1;245(3):339–348. doi: 10.1007/BF00290114. [DOI] [PubMed] [Google Scholar]
  14. Kinsey J. A., Helber J. Isolation of a transposable element from Neurospora crassa. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1929–1933. doi: 10.1073/pnas.86.6.1929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kinsey J. A. Transnuclear retrotransposition of the Tad element of Neurospora. Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9384–9387. doi: 10.1073/pnas.90.20.9384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kirk T. K., Farrell R. L. Enzymatic "combustion": the microbial degradation of lignin. Annu Rev Microbiol. 1987;41:465–505. doi: 10.1146/annurev.mi.41.100187.002341. [DOI] [PubMed] [Google Scholar]
  17. Leisola M. S., Kozulic B., Meussdoerffer F., Fiechter A. Homology among multiple extracellular peroxidases from Phanerochaete chrysosporium. J Biol Chem. 1987 Jan 5;262(1):419–424. [PubMed] [Google Scholar]
  18. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  19. McHale M. T., Roberts I. N., Noble S. M., Beaumont C., Whitehead M. P., Seth D., Oliver R. P. CfT-I: an LTR-retrotransposon in Cladosporium fulvum, a fungal pathogen of tomato. Mol Gen Genet. 1992 Jun;233(3):337–347. doi: 10.1007/BF00265429. [DOI] [PubMed] [Google Scholar]
  20. Ollikka P., Alhonmäki K., Leppänen V. M., Glumoff T., Raijola T., Suominen I. Decolorization of Azo, Triphenyl Methane, Heterocyclic, and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 Dec;59(12):4010–4016. doi: 10.1128/aem.59.12.4010-4016.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Radice A. D., Bugaj B., Fitch D. H., Emmons S. W. Widespread occurrence of the Tc1 transposon family: Tc1-like transposons from teleost fish. Mol Gen Genet. 1994 Sep 28;244(6):606–612. doi: 10.1007/BF00282750. [DOI] [PubMed] [Google Scholar]
  22. Raeder U., Thompson W., Broda P. Genetic factors influencing lignin peroxidase activity in Phanerochaete chrysosporium ME446. Mol Microbiol. 1989 Jul;3(7):919–924. doi: 10.1111/j.1365-2958.1989.tb00241.x. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Schalch H., Gaskell J., Smith T. L., Cullen D. Molecular cloning and sequences of lignin peroxidase genes of Phanerochaete chrysosporium. Mol Cell Biol. 1989 Jun;9(6):2743–2747. doi: 10.1128/mcb.9.6.2743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Timberlake W. E., Barnard E. C. Organization of a gene cluster expressed specifically in the asexual spores of A. nidulans. Cell. 1981 Oct;26(1 Pt 1):29–37. doi: 10.1016/0092-8674(81)90030-1. [DOI] [PubMed] [Google Scholar]
  28. Wallace R. B., Miyada C. G. Oligonucleotide probes for the screening of recombinant DNA libraries. Methods Enzymol. 1987;152:432–442. doi: 10.1016/0076-6879(87)52050-x. [DOI] [PubMed] [Google Scholar]
  29. Wilbur W. J., Lipman D. J. Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci U S A. 1983 Feb;80(3):726–730. doi: 10.1073/pnas.80.3.726. [DOI] [PMC free article] [PubMed] [Google Scholar]

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