Asgher M, Bhatti HN, Ashraf M, Legge RL. Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system. Biodegradation. 2008;19(6):771–83. https://doi.org/10.1007/s10532-008-9185-3.
Pollegioni L, Tonin F, Rosini E. Lignin-degrading enzymes. FEBS J. 2015;282(7):1190–213. https://doi.org/10.1111/febs.13224.
Knežević A, Stajić M, Milovanović I, Vukojević J. Degradation of beech wood and wheat straw by Trametes gibbosa. Wood Sci Technol. 2017;51(5):1227–47.
Berrin JG, Navarro D, Couturier M, Olive C, Grisel S, Haon M, et al. Exploring the natural fungal biodiversity of tropical and temperate forests toward improvement of biomass conversion. Appl Environ Microbiol. 2012;78(18):6483–90. https://doi.org/10.1128/AEM.01651-12.
Levasseur A, Piumi F, Coutinho PM, Rancurel C, Asther M, Delattre M, et al. FOLy: an integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds. Fungal Genet Biol. 2008;45(5):638–45. https://doi.org/10.1016/j.fgb.2008.01.004.
Janusz G, Pawlik A, Sulej J, Swiderska-Burek U, Jarosz-Wilkolazka A, Paszczynski A. Lignin degradation: microorganisms, enzymes involved, genomes analysis and evolution. FEMS Microbiol Rev. 2017;41(6):941–62. https://doi.org/10.1093/femsre/fux049.
Chi YJ, Zhang J. Gene expression of the white-rot fungus Lenzites gibbosa during wood degradation. Mycologia. 2022:1–16. https://doi.org/10.1080/00275514.2022.2072148.
Dittmer NT, Suderman RJ, Jiang H, Zhu YC, Gorman MJ, Kramer KJ, et al. Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect Biochem Mol Biol. 2004;34(1):29–41. https://doi.org/10.1016/j.ibmb.2003.08.003.
Baldrian P. Fungal laccases - occurrence and properties. FEMS Microbiol Rev. 2006;30(2):215–42. https://doi.org/10.1111/j.1574-4976.2005.00010.x.
Sharma P, Goel R, Capalash N. Bacterial laccases. World J Microbiol Biotechnol. 2007;23:823–32. https://doi.org/10.1007/s11274-006-9305-3.
Lu S, Li Q, Wei H, Chang MJ, Tunlaya-Anukit S, Kim H, et al. Ptr-miR397a is a negative regulator of laccase genes affecting lignin content in Populus trichocarpa. Proc Natl Acad Sci U S A. 2013;110(26):10848–53. https://doi.org/10.1073/pnas.1308936110.
Yan L, Xu R, Bian Y, Li H, Zhou Y. Expression profile of laccase gene family in white-rot basidiomycete Lentinula edodes under different environmental stresses. Genes (Basel). 2019;10(12). https://doi.org/10.3390/genes10121045.
Giardina P, Faraco V, Pezzella C, Piscitelli A, Vanhulle S, Sannia G. Laccases: a never-ending story. Cell Mol Life Sci. 2010;67(3):369–85. https://doi.org/10.1007/s00018-009-0169-1.
Piscitelli A, Pezzella C, Giardina P, Faraco V, Giovanni S. Heterologous laccase production and its role in industrial applications. Bioeng Bugs. 2010;1(4):252–62. https://doi.org/10.4161/bbug.1.4.11438.
Bettin F, Cousseau F, Martins K, Boff NA, Zaccaria S, Moura da Silveira M, et al. Phenol removal by laccases and other phenol oxidases of Pleurotus sajor-caju PS-2001 in submerged cultivations and aqueous mixtures. J Environ Manage. 2019;236:581–90. https://doi.org/10.1016/j.jenvman.2019.02.011.
Ma X, Liu L, Li Q, Liu Y, Yi L, Ma L, et al. High-level expression of a bacterial laccase, CueO from Escherichia coli K12 in Pichia pastoris GS115 and its application on the decolorization of synthetic dyes. Enzyme Microb Technol. 2017;103:34–41. https://doi.org/10.1016/j.enzmictec.2017.04.004.
Liu Q, Liu J, Hong D, Sun K, Li S, Latif A, et al. Fungal laccase-triggered 17beta-estradiol humification kinetics and mechanisms in the presence of humic precursors. J Hazard Mater. 2021;412:125197. https://doi.org/10.1016/j.jhazmat.2021.125197.
Coconi Linares N, Fernandez F, Loske AM, Gomez-Lim MA. Enhanced delignification of lignocellulosic biomass by recombinant fungus Phanerochaete chrysosporium overexpressing laccases and peroxidases. J Mol Microbiol Biotechnol. 2018;28(1):1–13. https://doi.org/10.1159/000485976.
Liu W, Chao Y, Liu S, Bao H, Qian S. Molecular cloning and characterization of a laccase gene from the basidiomycete Fome lignosus and expression in Pichia pastoris. Appl Microbiol Biotechnol. 2003;63(2):174–81. https://doi.org/10.1007/s00253-003-1398-0.
Eggert C, LaFayette PR, Temp U, Eriksson KE, Dean JF. Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus. Appl Environ Microbiol. 1998;64(5):1766–72. https://doi.org/10.1128/AEM.64.5.1766-1772.1998.
Xiao YZ, Hong YZ, Li JF, Hang J, Tong PG, Fang W, et al. Cloning of novel laccase isozyme genes from Trametes sp. AH28–2 and analyses of their differential expression. Appl Microbiol Biotechnol. 2006;71(4):493–501. https://doi.org/10.1007/s00253-005-0188-2.
Janusz G, Kucharzyk KH, Pawlik A, Staszczak M, Paszczynski AJ. Fungal laccase, manganese peroxidase and lignin peroxidase: gene expression and regulation. Enzyme Microb Technol. 2013;52(1):1–12. https://doi.org/10.1016/j.enzmictec.2012.10.003.
Langfelder P, Horvath S. WGCNA: an R package for weighted correlation network analysis. BMC Bioinformatics. 2008;9:559. https://doi.org/10.1186/1471-2105-9-559.
Song ZY, Chao F, Zhuo ZY, Ma Z, Li WZ, Chen G. Identification of hub genes in prostate cancer using robust rank aggregation and weighted gene co-expression network analysis. Aging-Us. 2019;11(13):4736–56. https://doi.org/10.18632/aging.102087.
Zhang H, Fu Y, Guo H, Zhang L, Wang C, Song W, et al. Transcriptome and proteome-based network analysis reveals a model of gene activation in wheat resistance to stripe rust. Int J Mol Sci. 2019;20(5). https://doi.org/10.3390/ijms20051106.
Kong Y, Feng ZC, Zhang YL, Liu XF, Ma Y, Zhao ZM, et al. identification of immune-related genes contributing to the development of glioblastoma using weighted gene co-expression Network Analysis. Front Immunol. 2020;11. ARTN 1281. https://doi.org/10.3389/fimmu.2020.01281.
Vrsanska M, Voberkova S, Langer V, Palovcikova D, Moulick A, Adam V, et al. Induction of laccase, lignin peroxidase and manganese peroxidase activities in white-rot fungi using copper complexes. Molecules. 2016;21(11):1553. https://doi.org/10.3390/molecules21111553.
Sudarson J, Ramalingam S, Kishorekumar P, Venkatesan K. Expeditious quantification of lignocellulolytic enzymes from indigenous wood rot and litter degrading fungi from tropical dry evergreen forests of Tamil Nadu. Biotechnol Res Int. 2014;2014:127848. https://doi.org/10.1155/2014/127848.
Lin JF, Liu ZM, Chen XY, Guo LQ, Wang J. Evaluation of assay methods for determining fungal laccase activity. Chin J Bioprocess Eng. 2009;7(4):1–8.
Gao C, Fu Q, Su B, Zhou S, Liu F, Song L, et al. Transcriptomic profiling revealed the signatures of intestinal barrier alteration and pathogen entry in turbot (Scophthalmus maximus) following Vibrio anguillarum challenge. Dev Comp Immunol. 2016;65:159–68. https://doi.org/10.1016/j.dci.2016.07.007.
Kim D, Pertea G, Trapnell C, Pimentel H, Kelley R, Salzberg SL. TopHat2: accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions. Genome Biol. 2013;14(4):R36. https://doi.org/10.1186/gb-2013-14-4-r36.
Hage H, Miyauchi S, Viragh M, Drula E, Min B, Chaduli D, et al. Gene family expansions and transcriptome signatures uncover fungal adaptations to wood decay. Environ Microbiol. 2021;23(10):5716–32. https://doi.org/10.1111/1462-2920.15423.
Florea L, Song L, Salzberg SL. Thousands of exon skipping events differentiate among splicing patterns in sixteen human tissues. F1000Res. 2013;2:188. https://doi.org/10.12688/f1000research.2-188.v2.
Ullmannova V, Haskovec C. The use of housekeeping genes (HKG) as an internal control for the detection of gene expression by quantitative real-time RT-PCR. Folia Biol-Prague. 2003;49(6):211–6.
Wang N, Wang R, Wang R, Chen S. Transcriptomics analysis revealing candidate networks and genes for the body size sexual dimorphism of Chinese tongue sole (Cynoglossus semilaevis). Funct Integr Genomics. 2018;18(3):327–39. https://doi.org/10.1007/s10142-018-0595-y.
Lou Y, Tian GY, Song Y, Liu YL, Chen YD, Shi JP, et al. Characterization of transcriptional modules related to fibrosing-NAFLD progression. Sci Rep. 2017;7(1):4748. https://doi.org/10.1038/s41598-017-05044-2.
Jin J, Tian F, Yang DC, Meng YQ, Kong L, Luo J, et al. PlantTFDB 4.0: toward a central hub for transcription factors and regulatory interactions in plants. Nucleic Acids Res. 2017;45(D1):D1040–5. https://doi.org/10.1093/nar/gkw982.
Omura T. Forty years of cytochrome P450. Biochem Biophys Res Commun. 1999;266(3):690–8. https://doi.org/10.1006/bbrc.1999.1887.
Sun J, Zhang T, Li Y, Wang X, Chen J. Functional characterization of the ABC transporter TaPdr2 in the tolerance of biocontrol the fungus Trichoderma atroviride T23 to dichlorvos stress. Biol Control. 2019;129:102–8. https://doi.org/10.1016/j.biocontrol.2018.10.004.
Ferreira P, Carro J, Serrano A, Martinez AT. A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes. Mycologia. 2015;107(6):1105–19. https://doi.org/10.3852/15-027.
Kracher D, Scheiblbrandner S, Felice AK, Breslmayr E, Preims M, Ludwicka K, et al. Extracellular electron transfer systems fuel cellulose oxidative degradation. Science. 2016;352(6289):1098–101. https://doi.org/10.1126/science.aaf3165.
Matsuzaki F, Shimizu M, Wariishi H. Proteomic and metabolomic analyses of the white-rot fungus Phanerochaete chrysosporium exposed to exogenous benzoic acid. J Proteome Res. 2008;7(6):2342–50. https://doi.org/10.1021/pr700617s.
Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D. Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proc Natl Acad Sci U S A. 1998;95(22):12838–43. https://doi.org/10.1073/pnas.95.22.12838.
留言 (0)