Структурно-генетическая организация лакказ базидиальных грибов

Список литературы

1. Nitta, К., К. Kataoka, and Т. Sakurai, Primary structure of a Japanese lacquer tree laccase as a prototype enzyme of multicopper oxidases. J Inorg Biochem, 2002. 91(1): p. 125−31.
2. Hoegger, P.J., et al., Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. FEBS J, 2006. 273(10): p. 2308−26.
3. Valderrama, В., et al., Evolutionary and structural diversity of fungal laccases. Antonie Van Leeuwenhoek, 2003. 84(4): p. 289−99.
4. Claus, H., Laccases and their occurrence in prokaryotes. Arch Microbiol, 2003. 179(3): p. 145−50.
5. Ullrich, R. and M. Hofrichter, Enzymatic hydroxylation of aromatic compounds. Cell Mol Life Sci, 2007. 64(3): p. 271−93.
6. Baldrian, P., Fungal laccases occurrence and properties. FEMS Microbiol Rev, 2006. 30(2): p. 215−42.
7. Kunamneni, A., et al., Laccases and their applications: a patent review. Recent Pat Biotechnol, 2008. 2(1): p. 10−24.
8. Mayer, A.M. and R.C. Staples, Laccase: new functions for an old enzyme. Phytochemistry, 2002. 60(6): p. 551−65.
9. Xu, F., et al., Site-directed mutations in fungal laccase: effect on redox potential, activity andpHprofile. Biochem J, 1998. 334 (Pt 1): p. 6370.
10. Nakamura, К. and N. Go, Function and molecular evolution of multicopper blue proteins. Cell Mol Life Sci, 2005. 62(18): p. 2050−66.
11. Suzuki, S., K. Kataoka, and K. Yamaguchi, Metal coordination and mechanism of multicopper nitrite reductase. Acc Chem Res, 2000. 33(10): p. 728−35.
12. Sakurai, T. and K. Kataoka, Structure and function of type I copper in multicopper oxidases. Cell Mol Life Sci, 2007. 64(19−20): p. 2642−56.
13. Brissos, V., et al., Expression system of CotA-laccase for directed evolution and high-throughput screenings for the oxidation of high-redox potential dyes. Biotechnol J, 2009.
14. Enguita, F.J., et al., Subsfrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis. J Biol Chem, 2004. 279(22): p. 23 472−6.
15. Tanaka, A., et al., Static and kinetic studies on the binding of Streptomyces trehalose inhibitor SGI with Rhizopus glucoamylase. Comparison with glucose and gluconolactone. J Biochem, 1982. 91(1): p. 1−9.
16. Askwith, C., et al., The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell, 1994. 76(2): p. 403−10.
17. Dancis, A., et al., Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell, 1994. 76(2): p. 393−402.
18. Rensing, С. and G. Grass, Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol Rev, 2003. 27(2−3): p. 197−213.
19. Kosman, D.J., FET3P, ceruloplasmin, and the role of copper in iron metabolism. Adv Protein Chem, 2002. 60: p. 221−69.
20. Francis, C.A. and B.M. Tebo, cumA multicopper oxidase genes from diverse Mn (II)-oxidizing and non-Mn (II) -oxidizing Pseudomonas strains. Appl Environ Microbiol, 2001. 67(9): p. 4272−8.
21. Wu, W.S., W.H. Li, and B.S. Chen, Computational reconstruction of transcriptional regulatory modules of the yeast cell cycle. BMC Bioinformatics, 2006. 7: p. 421.
22. Webb, S.M., et al., Evidence for the presence of Mn (III) intermediates in the bacterial oxidation of Mn (II). Proc Natl Acad Sci USA, 2005. 102(15): p. 5558−63.
23. Silver, S. and G. Ji, Newer systems for bacterial resistances to toxic heavy metals. Environ Health Perspect, 1994. 102 Suppl 3: p. 107−13.
24. Sakurai, T. and K. Kataoka, Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem Rec, 2007. 7(4): p. 220−9.
25. Kataoka, K., et al., Structure and function of the engineered multicopper oxidase CueO from Escherichia coli—deletion of the methionine-rich helical region covering the substrate-binding site. J MolBiol, 2007. 373(1): p. 141−52.
26. Farver, О., et al., The effect of driving force on intramolecular electron transfer in proteins. Studies on single-site mutated azurins. Eur J Biochem, 1992. 210(2): p. 399−403.
27. Liso, R., et al., Localization of ascorbic acid, ascorbic acid oxidase, and glutathione in roots of Cucurbita maxima L. J Exp Bot, 2004. 55(408): p. 2589−97.
28. Messerschmidt, A. and R. Huber, The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur J Biochem, 1990. 187(2): p. 341−52.
29. Pignocchi, C., et al., The function of ascorbate oxidase in tobacco. Plant Physiol, 2003. 132(3): p. 1631−41.
30. Wilson, J.X., Mechanism of action of vitamin С in sepsis: ascorbate modulates redox signaling in endothelium. Biofactors, 2009. 35(1): p. 5−13.
31. Messerschmidt, A., et al., X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. J Mol Biol, 1989. 206(3): p. 51 329.
32. Santagostini, L., et al., Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies. Int J Biochem Cell Biol, 2004. 36(5): p. 881−92.
33. Mei, G., et al., Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase. Biochemistry, 1997. 36(36): p. 10 917−22.
34. Holmberg, C.G., On the presence of a laccase-like enzyme in serum and its relation to the copper in serum. Acta Physiol. Scand, 1944. 8: p. 227−229.
35. Holmberg, C.G. and C.B. Laurell, Investigation in serum copper. Acta Chem. Scand., 1948. 2: p. 550−556. .
36. Osaki, S., Kinetic studies of ferrous ion oxidation with crystalline human ferrooxidase (ceruloplasmin). J. Biol. Chem., 1966. 241: p. 5053−5059.
37. Mukhopadhyay, C.K., et al., Identification of the prooxidant site of human ceruloplasmin: a model for oxidative damage by copper bound to protein surfaces. Proc Natl Acad Sci USA, 1997. 94(21): p. 1 154 651.
38. Vachette, P., et al., A key structural role for active site type 3 copper ions in human ceruloplasmin. J Biol Chem, 2002. 277(43): p. 40 823−31.
39. Hellman, N.E. and J.D. Gitlin, Ceruloplasmin metabolism and function. Annu Rev Nutr, 2002. 22: p. 439−58.
40. Hellman, N.E., et al., Mechanisms of copper incorporation into human ceruloplasmin. J Biol Chem, 2002. 277(48): p. 46 632−8.
41. Texel, S.J., X. Xu, and Z.L. Harris, Ceruloplasmin in neurodegenerative diseases. Biochem Soc Trans, 2008. 36(Pt 6): p. 1277−81.
42. Healy, J. and K. Tipton, Ceruloplasmin and what it might do. J Neural Transm, 2007. 114(6): p. 777−81.
43. Vassiliev, V., Z.L. Harris, and P. Zatta, Ceruloplasmin in neurodegenerative diseases. Brain Res Brain Res Rev, 2005. 49(3): p. 633−40.
44. Ryden, L., Human ceruloplasmin as a polymorphic glycoprotein. Tryptic glycopeptides from two forms of the protein. Int J Protein Res, 1971. 3(4): p. 191−200.
45. Magdoff-Fairchild, В., F.M. Lovell, and B.W. Low, An x-ray crystallographic study of ceruloplasmin. Determination of molecular weight. J Biol Chem, 1969. 244(13): p. 3497−9.
46. Broman, L., Separation and characterization of two coeruloplasmins from human serum. Nature, 1958. 182(4650): p. 1655−7.
47. Ortel, T.L., N. Takahashi, and F.W. Putnam, Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains. Proc Natl Acad Sci U S A, 1984. 81(15): p. 4761−5.
48. Boivin, S., et al., Molecular characterization of human and bovine ceruloplasmin using MALDI-TOF mass spectrometry. Biochem Biophys Res Commun, 2001. 288(4): p. 1006−10.
49. Ryan, T.P., T.A. Grover, and S.D. Aust, Rat ceruloplasmin: resistance to proteolysis and kinetic comparison with human ceruloplasmin. Arch Biochem Biophys, 1992. 293(1): p. 1−8.
50. Cappelli-Bigazzi, M., et al., Ceruloplasmin impairs endothelium-dependent relaxation of rabbit aorta. Am J Physiol, 1997. 273(6 Pt 2): p. H2843−9.
51. Bielli, P. and L. Calabrese, Structure to function relationships in ceruloplasmin: a 'moonlighting'protein. CellMol Life Sci, 2002. 59(9): p. 1413−27.
52. Grossmann, J.G., et al., X-ray absorption studies and homology modeling define the structural features that specify the nature of the copper site in rusticyanin. Biochemistry, 1995. 34(26): p. 8406−14.
53. Munoz, C., et al., Laccase isoenzymes of Pleurotus eryngii: characterization, catalytic properties, and participation in activation of molecular oxygen and Mn2+ oxidation. Appl Environ Microbiol, 1997. 63(6): p. 2166−74.
54. Guillen, F., et al., Quinone redox cycling in the ligninolytic fungus Pleurotus eryngii leading to extracellular production of superoxide anion radical. Arch Biochem Biophys, 1997. 339(1): p. 190−9.
55. Munoz, C., et al., Induction and Characterization of Laccase in the Ligninolytic Fungus Pleurotus eryngii. Curr Microbiol, 1997. 34(1): p. 1−5.
56. Shleev, S.V., et al., Comparison of physico-chemical characteristics of four laccases from different basidiomycetes. Biochimie, 2004. 86(9−10): p. 693−703.
57. Slomczynski, D., J.P. Nakas, and S.W. Tanenbaum, Production and Characterization of Laccase from Botrytis cinerea 61−34. Appl Environ Microbiol, 1995. 61(3): p. 907−912.
58. Kawasaki, N., et al., The significance of glycosylation analysis in development of biopharmaceuticals. Biol Pharm Bull, 2009. 32(5): p. 796−800.
59. Cambria, M., et al., Production, purification, and properties of an extracellular laccase from Rigidoporus lignosus. Protein Expr Purif, 2000. 18(2): p. 141−7.
60. Palmieri, G., et al., Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus. Appl Environ Microbiol, 2000. 66(3): p. 920−4.
61. Fernandez-Larrea, J. and U. Stahl, Isolation and characterization of a laccase gene from Podospora anserina. Mol Gen Genet, 1996. 252(5): p. 539−51.
62. Bollag, J.M. and A. Leonowicz, Comparative Studies of Extracellular Fungal Laccases. Appl Environ Microbiol, 1984. 48(4): p. 849−854.
63. Morozova, O.V., et al., «Blue» laccases. Biochemistry (Mosc), 2007. 72(10): p. 1136−50.
64. Xu, F., et al., Targeted mutations in a Trametes villosa laccase. Axial perturbations of the T1 copper. J Biol Chem, 1999. 274(18): p. 123 725.
65. Bourbonnais, R., et al., Reactivities of Various Mediators and Laccases with Kraft Pulp and Lignin Model Compounds. Appl Environ Microbiol, 1997. 63(12): p. 4627−4632.
66. Giardina, P., et al., Cloning and sequencing of a laccase gene from the lignin-degrading basidiomycete Pleurotus ostreatus. Appl Environ Microbiol, 1995. 61(6): p. 2408−13.
67. Giardina, P., et al., The gene, protein and glycan structures of laccase from Pleurotus ostreatus. Eur J Biochem, 1996. 235(3): p. 508−15.
68. Palmieri, G., et al., A novel white laccase from Pleurotus ostreatus. J Biol Chem, 1997. 272(50): p. 31 301−7.
69. Giardina, P., et al., Protein and gene structure of a blue laccase from Pleurotus ostreatusl. Biochem J, 1999. 341 (Pt3): p. 655−63.
70. Zumarraga, M., et al., Altering the laccase functionality by in vivo assembly of mutant libraries with different mutational spectra. Proteins, 2008. 71(1): p. 250−60.
71. Pezzella, C., et al., The Pleurotus ostreatus laccase multi-gene family: isolation and heterologous expression of new family members. Curr Genet, 2009. 55(1): p. 45−57.
72. Cullen, D., Recent advances on the molecular genetics of ligninolytic fungi. J Biotechnol, 1997. 53(2−3): p. 273−89.
73. Lomascolo, A., et al., Basidiomycetes as new biotechnological tools to generate natural aromatic flavours for the food industry. Trends Biotechnol, 1999. 17(7): p. 282−9.
74. Eggert, C., U. Temp, and K.E. Eriksson, Laccase is essential for lignin degradation by the white-rot fungus Pycnoporus cinnabarinus. FEBS Lett, 1997. 407(1): p. 89−92.
75. Bajpai, P., A. Anand, and P.K. Bajpai, Bleaching with lignin-oxidizing enzymes. Biotechnol AnnuRev, 2006. 12: p. 349−78.
76. Garrett, T.P., et al., The ciystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide. J Biol Chem, 1984. 259(5): p. 2822−5.
77. Palmer, A.E., et al., Spectroscopic characterization and 02 reactivity of the trinuclear Си cluster of mutants of the multicopper oxidase Fet3p. Biochemistry, 2002. 41(20): p. 6438−48.
78. Palmer, A.E., et al., Spectroscopic characterization of the Leu513His variant offungal laccase: effect of increased axial ligand interaction on the geometric and electronic structure of the type 1 Си site. Inorg Chem, 2003. 42(13): p. 4006−17.
79. Solomon, E.I., et al., 02 and N20 activation by Bi-, Tri-, and teti-anuclear Си clusters in biology. Acc Chem Res, 2007. 40(7): p. 581−91.
80. Fraterrigo, T.L., et al., Which copper is paramagnetic in the type 2/type 3 cluster of laccase? J Biol Inorg Chem, 1999. 4(2): p. 183−7.
81. Adman, E.T., Copper protein structures. Adv Protein Chem, 1991. 42: p. 145−97.
82. Huang, H.W., et al., Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements. Biochim Biophys Acta, 1998. 1384(1): p. 160−70.
83. Augustine, A.J., et al., Spectroscopic and kinetic studies of perturbed trinuclear copper clusters: the role of protons in reductive cleavage of the O-O bond in the multicopper oxidase Fet3p. J Am Chem Soc, 2007. 129(43): p. 13 118−26.
84. Peyratout, C.S., et al., EPR studies of ligand binding to the type 2/type 3 cluster in tree laccase. Arch Biochem Biophys, 1994. 314(2): p. 40 511.
85. Enguita, F.J., et al., Structural Characterization of a Bacterial Laccase Reaction Cycle. To be Published.
86. Lu, H., et al., Reversible translocation of glycoprotein lb in plasmin-treated platelets: consequences for platelet function. Eur J Clin Invest, 1993. 23(12): p. 785−93.
87. Dawson, K.A., M.C. Preziosi, and D.R. Caldwell, Some effects of uncouplers and inhibitors on growth and electron transport in rumen bacteria. J Bacterid, 1979. 139(2): p. 384−92.
88. Sakurai, Т., Kinetics of electron transfer between cytochrome с and laccase. Biochemistry, 1992. 31(40): p. 9844−7.
89. Sakurai, T. and J. Takahashi, EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase. Biochim Biophys Acta, 1995. 1248(2): p. 143−8.
90. Quintanar, L., et al., Shall we dance? How a multicopper oxidase chooses its electron transfer partner. Acc Chem Res, 2007. 40(6): p. 445−52.
91. Ducros, V., et al., Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Си-depleted' isoforms. Acta Crystallogr D Biol Crystallogr., 2001. D57: p. 333−336.
92. Beratan, D.N., et al., Electron-tunneling pathways in proteins. Science, 1992. 258(5089): p. 1740−1.
93. Hakulinen, N., et al., A near atomic resolution structure of a Melanocarpus albomyces laccase. Journal of Structural Biology, 2008. 162(1): p. 29−39.
94. Bento, I., et al., Dioxygen reduction by multi-copper oxidases- a structural perspective. Dalton Trans, 2005(21): p. 3507−13.
95. Castilho, F.J., et al., On the diversity of the laccase gene: a phylogenetic perspective from Botryosphaeria rhodina (Ascomycota: Fungi) and other related taxa. Biochem Genet, 2009. 47(1−2): p. 80−91.
96. Ducros, V., et al., Crystal structure of the type-2 Си depleted laccase from Coprinus cinereus at 2.2 A resolution. Nat Struct Biol, 1998. 5(4): p. 310−6.
97. Hakulinen, N., et al., Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat Struct Biol, 2002. 9(8): p. 601−5.
98. Ferraroni, M., et al., Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases. BMC Struct Biol, 2007. 7: p. 60.
99. Garavaglia, S., et al., The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. J Mol Biol, 2004. 342(5): p. 151 931.
100. Piontek, К., M. Antorini, and Т. Choinowski, Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J Biol Chem, 2002. 277(40): p. 37 663−9.
101. Ducros, V., et al., Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Си-depleted' isoforms. Acta Crystallogr D Biol Crystallogr, 2001. 57(Pt 2): p. 333−6.
102. Lyashenko, A.V., et al., Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima. Acta Crystallogr SectF Struct Biol Cryst Commun, 2006. 62(Pt 10): p. 954−7.
103. Polyakov, K.M., et al., Structure of native laccase from Trametes hirsuta at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr, 2009. 65(Pt 6): p. 611−7.
104. Enguita, F.J., et al., Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties. J Biol Chem, 2003. 278(21): p. 19 416−25.
105. Skalova, Т., et al., The structure of the small laccase from Streptomyces coelicolor reveals a link between laccases and nitrite reductases. J Mol Biol, 2009. 385(4): p. 1165−78.
106. Hakulinen, N., et al., A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase. Biochem Biophys Res Commun, 2006. 350(4): p. 929−34.
107. Ong, E., W.B. Pollock, and M. Smith, Cloning and sequence analysis of two laccase complementary DNAs from the ligninolytic basidiomycete Trametes versicolor. Gene, 1997. 196(1−2): p. 113−9.
108. Yaver, D.S., et al., Purification, characterization, molecular cloning, and expression of two laccase genes from the white rot basidiomycete Trametes villosa. Appl Environ Microbiol, 1996. 62(3): p. 834−41.
109. Wahleithner, J. A., et al., The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani. Curr Genet, 1996. 29(4): p. 395−403.
110. Collins, P.J. and A. Dobson, Regulation of Laccase Gene Transcription in Trametes versicolor. Appl Environ Microbiol, 1997. 63(9): p. 34 443 450.
111. Yaver, D.S. and E.J. Golightly, Cloning and characterization of three laccase genes from the white-rot basidiomycete Trametes villosa: genomic organization of the laccase gene family. Gene, 1996. 181(1−2): p. 95−102.
112. Hoegger, P. J., et al., The laccase gene family in Coprinopsis cinerea (Coprinus cinereus). Curr Genet, 2004. 45(1): p. 9−18.
113. Kiiskinen, L.L., M. Ratto, and K. Kruus, Screening for novel laccase-producing microbes. J Appl Microbiol, 2004. 97(3): p. 640−6.
114. Baralle, D. and M. Baralle, Splicing in action: assessing disease causing sequence changes. J Med Genet, 2005. 42(10): p. 737−48.
115. Patthy, L., Intron-dependent evolution: preferred types of exons and introns. FEBS Lett, 1987. 214(1): p. 1−7.
116. Rogozin, I.B., et al., Analysis of evolution of exon-intron structure of eukaryotic genes. Brief Bioinform, 2005. 6(2): p. 118−34.
117. Ochman, H., A.S. Gerber, and D.L. Hartl, Genetic applications of an inverse polymerase chain reaction. Genetics, 1988. 120(3): p. 621−3.
118. Quaratino, D., et al., Production, purification and partial characterisation of a novel laccase from the white-rot fungus Panus tigrinus CBS 577.79. Antonie Van Leeuwenhoek, 2007. 91(1): p. 57−69.
119. D’Souza, T.M., K. Boominathan, and C.A. Reddy, Isolation of laccase gene-specific sequences from white rot and brown rot fungi by PCR. Appl Environ Microbiol, 1996. 62(10): p. 3739−44.
120. Liu, W., et al., Molecular cloning and characterization of a laccase gene from the basidiomycete Fome lignosus and expression in Pichia pastoris. Appl Microbiol Biotechnol, 2003. 63(2): p. 174−81.
121. Bonomo, R.P., et al., A comparative study of two isoforms of laccase secreted by the «white-rot» fungus Rigidoporus lignosus, exhibiting significant structural and functional differences. J Inorg Biochem, 1998. 71(3−4): p. 205−11.
122. Nicole, M., et al., Immunocytochemical localization of laccase LI in wood decayed by Rigidoporus lignosus. Appl Environ Microbiol, 1992. 58(5): p. 1727−39.
123. Heinzkill, M., et al., Characterization oflaccases and peroxidases from wood-rotting fungi (family Coprinaceae). Appl Environ Microbiol, 1998. 64(5): p. 1601−6.
124. Joo, S.S., et al., Molecular cloning and expression of a laccase from Ganoderma lucidum, and its antioxidative properties. Mol Cells, 2008. 25(1): p. 112−8.
125. Hellman, N.E., et al., Biochemical analysis of a missense mutation in aceruloplasminemia. J Biol Chem, 2002. 277(2): p. 1375−80.
126. Jasalavich, C.A., A. Ostrofsky, and J. Jellison, Detection and identification of decay fungi in spruce wood by restriction fragment length polymorphism analysis of amplified genes encoding rRNA. Appl Environ Microbiol, 2000. 66(11): p. 4725−34.
127. Lyashenko, A.V., et al., X-ray structural studies of the fungal laccase from Cerrena maxima. J Biol Inorg Chem, 2006. 11(8): p. 963−73.1. БЛАГОДАРНОСТИ
128. Автор выражает глубокую признательность:
129. Полякову К.М. ст.н.с. Института молекулярной биологии им. В. А. Энгельгардта РАН за оказанную помощь в проведении анализа структур лакказ.
130. Упорову И. В ст.н.с. кафедры химической энзимологии Химического факультета МГУ имени М. В. Ломоносова за помощь в проведении математического моделирования структур лакказ.
131. Рожковой A.M. н.с. Института биохимии имени А. Н. Баха РАН за оказанную помощь в проведении экспериментов по клонированию генов лакказ.