This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Eggert, C.
Right arrow Articles by Dean, J. F. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Eggert, C.
Right arrow Articles by Dean, J. F. D.
Agricola
Right arrow Articles by Eggert, C.
Right arrow Articles by Dean, J. F. D.

 Previous Article  |  Next Article 

Appl Environ Microbiol, May 1998, p. 1766-1772, Vol. 64, No. 5
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Molecular Analysis of a Laccase Gene from the White Rot Fungus Pycnoporus cinnabarinus

Claudia Eggert,1,* Peter R. LaFayette,2 Ulrike Temp,1 Karl-Erik L. Eriksson,3 and Jeffrey F. D. Dean2

Institute of General and Microbial Genetics, Friedrich-Schiller University of Jena, 07743 Jena, Germany,1 and Department of Biochemistry and Molecular Biology, Center for Biological Resource Recovery,3 and Warnell School of Forest Resources,2 University of Georgia, Athens, Georgia 30602

Received 1 December 1997/Accepted 20 February 1998

It was recently shown that the white rot basidiomycete Pycnoporus cinnabarinus secretes an unusual set of phenoloxidases when it is grown under conditions that stimulate ligninolysis (C. Eggert, U. Temp, and K.-E. L. Eriksson, Appl. Environ. Microbiol. 62:1151-1158, 1996). In this report we describe the results of a cloning and structural analysis of the laccase-encoding gene (lcc3-1) expressed by P. cinnabarinus during growth under xylidine-induced conditions. The coding region of the genomic laccase sequence, which is preceded by the eukaryotic promoter elements TATA and CAATA, spans more than 2,390 bp. The corresponding laccase cDNA was identical to the genomic sequence except for 10 introns that were 50 to 60 bp long. A sequence analysis indicated that the P. cinnabarinus lcc3-1 product has a Phe residue at a position likely to influence the reduction-oxidation potential of the enzyme's type 1 copper center. The P. cinnabarinus lcc3-1 sequence was most similar to the sequence encoding a laccase from Coriolus hirsutus (level of similarity, 84%).

* Corresponding author. Mailing address: Institute of General Microbiology and Microbial Genetics, Friedrich-Schiller University of Jena, Neugasse 24, D-07743 Jena, Germany. Phone and fax: (49) 3641-949327. E-mail: Claudia.Eggert{at}uni-jena.de.

Appl Environ Microbiol, May 1998, p. 1766-1772, Vol. 64, No. 5
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Taprab, Y., Johjima, T., Maeda, Y., Moriya, S., Trakulnaleamsai, S., Noparatnaraporn, N., Ohkuma, M., Kudo, T. (2005). Symbiotic Fungi Produce Laccases Potentially Involved in Phenol Degradation in Fungus Combs of Fungus-Growing Termites in Thailand. Appl. Environ. Microbiol. 71: 7696-7704 [Abstract] [Full Text]  
  • Alves, A. M. C. R., Record, E., Lomascolo, A., Scholtmeijer, K., Asther, M., Wessels, J. G. H., Wosten, H. A. B. (2004). Highly Efficient Production of Laccase by the Basidiomycete Pycnoporus cinnabarinus. Appl. Environ. Microbiol. 70: 6379-6384 [Abstract] [Full Text]  
  • Kiiskinen, L.-L., Saloheimo, M. (2004). Molecular Cloning and Expression in Saccharomyces cerevisiae of a Laccase Gene from the Ascomycete Melanocarpus albomyces. Appl. Environ. Microbiol. 70: 137-144 [Abstract] [Full Text]  
  • Soden, D. M., O'Callaghan, J., Dobson, A. D. W. (2002). Molecular cloning of a laccase isozyme gene from Pleurotus sajor-caju and expression in the heterologous Pichia pastoris host. Microbiology 148: 4003-4014 [Abstract] [Full Text]  
  • Galhaup, C., Goller, S., Peterbauer, C. K., Strauss, J., Haltrich, D. (2002). Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiology 148: 2159-2169 [Abstract] [Full Text]  
  • Soden, D. M., Dobson, A. D. W. (2001). Differential regulation of laccase gene expression in Pleurotus sajor-caju. Microbiology 147: 1755-1763 [Abstract] [Full Text]  
  • Zhao, J., Kwan, H. S. (1999). Characterization, Molecular Cloning, and Differential Expression Analysis of Laccase Genes from the Edible Mushroom Lentinula edodes. Appl. Environ. Microbiol. 65: 4908-4913 [Abstract] [Full Text]  
  • Yaver, D. S., Overjero, M. D. C., Xu, F., Nelson, B. A., Brown, K. M., Halkier, T., Bernauer, S., Brown, S. H., Kauppinen, S. (1999). Molecular Characterization of Laccase Genes from the Basidiomycete Coprinus cinereus and Heterologous Expression of the Laccase Lcc1. Appl. Environ. Microbiol. 65: 4943-4948 [Abstract] [Full Text]  
  • Xu, F., Palmer, A. E., Yaver, D. S., Berka, R. M., Gambetta, G. A., Brown, S. H., Solomon, E. I. (1999). Targeted Mutations in a Trametes villosa Laccase. AXIAL PERTURBATIONS OF THE T1 COPPER. J. Biol. Chem. 274: 12372-12375 [Abstract] [Full Text]  
  • Temp, U., Eggert, C. (1999). Novel Interaction between Laccase and Cellobiose Dehydrogenase during Pigment Synthesis in the White Rot Fungus Pycnoporus cinnabarinus. Appl. Environ. Microbiol. 65: 389-395 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»