{Reference Type}: Journal Article
{Author}: Nakade, Keiko; Nakagawa, Yuko; Yano, Akira; Konno, Naotake; Sato, Toshitsugu; Sakamoto, Yuichi
{Year}: 2013
{Title}: Effective induction of pblac1 laccase by copper ion in Polyporus brumalis ibrc05015
{Tag}: 0
{Star}: 0
{Journal}: FUNGAL BIOLOGY
{Volume}: 117
{Issue}: 1
{Pages}: 52-61
{ISBN/ISSN}: 1878-6146
{Keywords}: ACE1 TRANSCRIPTION FACTOR; BASIDIOMYCETE PHANEROCHAETE-CHRYSOSPORIUM; METALLOTHIONEIN GENE-TRANSCRIPTION; CU,ZN SUPEROXIDE-DISMUTASE; PLEUROTUS-SAJOR-CAJU; DNA-BINDING PROTEIN; SACCHAROMYCES-CEREVISIAE; TRAMETES SP; EXPRESSION; YEAST; Copper; High production of Lacs; Lac inducer; PbLac1; pblac1 promoter; Polyporus brumalis; Transcriptional factor Ace1
{Abstract}: Polyporus brumalis ibrc05015 is a strain capable of high laccase (Lac) production. Among several inducers, 0.25 mM copper was most effective for Lac production. One of the Lacs induced by copper was PbLac1, and its transcription was induced within 60 min after copper addition. The promoter region of pblac1 contained six putative metal response elements and one Ace1 consensus cis-element. We cloned the 13: brumalis PbAce1 transcription factor, a homologue of Saccharomyces cerevisiae transcription factor Ace1, which regulates metallothionein genes in response to excess copper. PbAce1 complemented the function of Ace1 in an S. cerevisiae Delta ace strain. The conserved N-terminal copper-fist DNA binding domain of PbAce1 was required for complementation. In the PbAce1 complemented Delta ace1 strain, the pblac1 promoter was constitutively expressed at a high level, independent of copper concentration. PbAce1 has two Cys-rich repeat motifs (PbC1 and PbC2), which are similar to the Cys-rich repeat domain in metallothionein proteins, and are uniquely conserved in the C-terminal domain of basidiomycetous Ace1 sequences. These C-terminal domains could be involved in copper sensing and concentration-dependent Lac production in basidiomycetous fungi. (C) 2012 The British Mycological Society. Published by Elsevier Ltd. All rights reserved.
{Author Address}: Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan; Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan; Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan; Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan; Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan; Iwate Biotechnol Res Ctr, Kitakami, Iwate 0240003, Japan
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Japan

{Reference Type}: Journal Article
{Author}: Makela, Miia R.; Lundell, Taina; Hatakka, Annele; Hilden, Kristiina
{Year}: 2013
{Title}: Effect of copper, nutrient nitrogen, and wood-supplement on the production of lignin-modifying enzymes by the white-rot fungus Phlebia radiata
{Tag}: 0
{Star}: 0
{Journal}: FUNGAL BIOLOGY
{Volume}: 117
{Issue}: 1
{Pages}: 62-70
{ISBN/ISSN}: 1878-6146
{Keywords}: BASIDIOMYCETE PHANEROCHAETE-CHRYSOSPORIUM; MANGANESE PEROXIDASE; LACCASE GENE; CERIPORIOPSIS-SUBVERMISPORA; DEGRADING BASIDIOMYCETE; PLEUROTUS-OSTREATUS; HETEROLOGOUS EXPRESSION; STRUCTURAL-ANALYSIS; MODEL COMPOUNDS; DEGRADATION; Basidiomycete; Laccase; Lignin-modifying peroxidases; White-rot fungi; Wood degradation
{Abstract}: Production of the oxidoreductive lignin-modifying enzymes - lignin and manganese peroxidases (MnPs), and laccase - of the white-rot basidiomycete Phlebia radiata was investigated in semi-solid cultures supplemented with milled grey alder or Norway spruce and charcoal. Concentrations of nutrient nitrogen and Cu-supplement varied also in the cultures. According to extracellular activities, production of both lignin peroxidase (LiP) and MnP was significantly promoted with wood as carbon source, with milled alder (MA) and low nitrogen (LN) resulting with the maximal LiP activities (550 nkat l(-1)) and noticeable levels of MnP (3 mu kat l(-1)). Activities of LiP and MnP were also elevated on high nitrogen (HN) complex medium when supplemented with spruce and charcoal. Maximal laccase activities (22 and 29 mu kat l(-1)) were obtained in extra high nitrogen (eHN) containing defined and complex media supplemented with 1.5 mM Cu2+. However, the nitrogen source, either peptone or ammonium nitrate and asparagine, caused no stimulation on laccase production without Cu-supplement. This is also the first report to demonstrate a new, on high Cu2+ amended medium produced extracellular laccase of P. radiata with pI value of 4.9, thereby complementing our previous findings on gene expression, and cloning of a second laccase of this fungus. (C) 2012 The British Mycological Society. Published by Elsevier Ltd. All rights reserved.
{Author Address}: Viikki Bioctr 1, Div Microbiol, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland; Viikki Bioctr 1, Div Microbiol, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland; Viikki Bioctr 1, Div Microbiol, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland; Viikki Bioctr 1, Div Microbiol, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Finland

{Reference Type}: Journal Article
{Author}: Yin, Yonggang; Liu, Yu; Wang, Shouxian; Zhao, Shuang; Xu, Feng
{Year}: 2013
{Title}: Examining genetic relationships of Chinese Pleurotus ostreatus cultivars by combined RAPD and SRAP markers
{URL}: http://www.sciencedirect.com/science/article/pii/S1340354012000344
{Tag}: 0
{Star}: 0
{Journal}: Mycoscience
{Volume}: 54
{Issue}: 3
{Pages}: 221-225
{Date Displayed}: 2013/5//
{Alternate Title}: Mycoscience
{ISBN/ISSN}: 1340-3540
{Keywords}: Genetic diversity; Molecular marker; Polymorphism; UPGMA
{Abstract}: Combined randomly amplified polymorphic DNA (RAPD) and sequence-related amplified polymorphism (SRAP) were used to assess the genetic diversity of Pleurotus ostreatus strains cultivated in China. For the RAPD and SRAP analyses, 479 and 282 polymorphic bands were obtained from 20 P. ostreatus strains using 20 and 13 selected primers or primer pairs, respectively. A combined RAPD/SRAP dendrogram grouped the 20 strains into five clades with a coefficient of 0.690. The comparison of RAPD and SRAP was evaluated in the present study. The combined RAPD/SRAP markers provided reliable information regarding the relationships among the P. ostreatus strains.

{Reference Type}: Journal Article
{Author}: Tasaki, Yuji; Toyama, Shungo; Kuribayashi, Takashi; Joh, Toshio
{Year}: 2013
{Title}: Molecular characterization of a lipoxygenase from the basidiomycete mushroom Pleurotus ostreatus
{Tag}: 0
{Star}: 0
{Place Published}: 2-4-16 Yayoi, Bunkyo-ku, Tokyo, 113, Japan
{Journal}: Bioscience, Biotechnology and Biochemistry
{Volume}: 77
{Issue}: 1
{Pages}: 38-45
{Date Displayed}: 2013
{ISBN/ISSN}: 09168451
{Original Publication}: Japan Soc. for Bioscience Biotechnology and Agrochemistry
{Keywords}: Fungi; Amino acids; Gene encoding
{Abstract}: The full-length cDNA of the gene PoLOX1 encoding a lipoxygenase (LOX) and its corresponding genomic DNA were isolated from the basidiomycete mushroom Pleurotus ostreatus strain H1. The deduced amino acid sequence of PoLOX1 showed similarity to a valencene dioxygenase of Pleurotus sapidus, putative LOX-like proteins from ascomycete, basidiomycete, and deuteromycete fungi, and known LOXs from plants, animals, and bacteria. PoLOX1 also contained the LOX ironbinding catalytic domain in the C-terminal region, but not the polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain, which is usually found in the N-terminal region of eukaryotic LOXs. Genomic sequence analysis revealed that PoLOX1 was interrupted by one intron, and that the promoter region included TATA and CAAT boxes. Southern blot analysis indicated that PoLOX1 is a member of a small gene family comprising highly similar genes. Northern blot analysis revealed that it is transcribed more abundantly in the stipes of the fruit bodies than in the caps.
{Notes}: Compilation and indexing terms, Copyright 2013 Elsevier Inc.
20130716025858
1-octen- 3-ol
Aroma
Lipoxygenases
Mushroom
Pleurotus ostreatus
{Author Address}: Department of Materials Engineering, Nagaoka National College of Technology, 888 Nishikatagai, Nagaoka, Niigata 940-8532, Japan