Characterization of a hydroxyl-radical-producing glycoprotein and its presumptive genes from the white-rot basidiomycete Phanerochaete chrysosporium

During wood decay, the white-rot basidiomycete Phanerochaete chrysosporium secretes low-molecular-mass glycoproteins that catalyze a redox reaction between O 2 and electron donors to produce hydroxyl radical. This reaction accounts for most of the hydroxyl radical produced in wood-degrading cultures...

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Bibliographic Details
Published in:	Journal of biotechnology Vol. 128; no. 3; pp. 500 - 511
Main Authors:	Tanaka, Hiromi, Yoshida, Gou, Baba, Yousuke, Matsumura, Kenta, Wasada, Hiroshi, Murata, Jirou, Agawa, Mana, Itakura, Shuji, Enoki, Akio
Format:	Journal Article
Language:	English
Published:	Lausanne Elsevier B.V 20-02-2007 Amsterdam Elsevier New York, NY
Subjects:	Amadori product Amino Acid Sequence amino acid sequences Base Sequence Basidiomycetes Biological and medical sciences Biotechnology Cloning, Molecular complementary DNA DNA, Complementary - analysis exons Fe(III) reduction free radicals Fundamental and applied biological sciences. Psychology fungal proteins Fungal Proteins - genetics Fungal Proteins - isolation & purification Fungal Proteins - metabolism genes Glycoprotein glycoproteins Glycoproteins - genetics Glycoproteins - isolation & purification Glycoproteins - metabolism Hydroxyl radical Hydroxyl Radical - metabolism hydroxyl radicals introns iron Models, Biological Molecular Sequence Data nucleotide sequences Phanerochaete - genetics Phanerochaete - metabolism Phanerochaete chrysosporium reactive oxygen species reduction Sequence Homology, Amino Acid LiP TBA TCA Fe(III) reduction Phanerochaete chrysosporium Glycoprotein Amadori product OH 5-HMF MnP Hydroxyl radical Fungi Characterization Reduction Gene Basidiomycetes Thallophyta
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Summary:	During wood decay, the white-rot basidiomycete Phanerochaete chrysosporium secretes low-molecular-mass glycoproteins that catalyze a redox reaction between O 2 and electron donors to produce hydroxyl radical. This reaction accounts for most of the hydroxyl radical produced in wood-degrading cultures of P. chrysosporium. In combination with phenol oxidases, hydroxyl radical is believed to play a role in lignin degradation. The secreted glycoproteins also reduce Fe(III) to Fe(II) and strongly bind Fe(II). The partially purified glycoproteins contain 1-amino-1-deoxy-2-ketose (ketoamine) produced by the condensation of side-chain amino groups and carbohydrate. cDNAs and two putative genes encoding these glycoproteins, glp1 and glp2, have been isolated and sequenced. The 875 bp glp1 and 864 bp glp2 are found on scaffold 2 of the P. chrysosporium genome. These presumptive genes each consist of seven introns and eight exons. The latter encode a predicted protein of 138 amino acids and a 22-amino-acid signal sequence for secretion. The predicted protein sequences are nearly identical to N-terminal and internal sequences obtained from the partially purified glycoprotein. The molecular masses of the deduced mature proteins, 13,981 ( glp1) and 13,970 ( glp2), coincide with the molecular mass of the glycoprotein as determined by tricine-SDS-PAGE.
Bibliography:	http://dx.doi.org/10.1016/j.jbiotec.2006.12.010 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0168-1656 1873-4863
DOI:	10.1016/j.jbiotec.2006.12.010