Abstract
The amatoxins, phallotoxins, cycloamanides, and antamanide belong to the special class of secondary metabolites known as cyclic peptides or cyclopeptides – strings of amino acids in which the N and C termini are joined head-to-tail by amide (peptide) bonds (Chap. 2). Cyclic peptides possess many chemical attributes that contribute to high biological activity, including chemical stability, membrane permeability, and rigidity. The importance of these attributes is discussed in more detail in Chap. 7. The focus of this chapter is the specific biological activities of the characterized cyclic peptides of Amanita and other mushrooms. The majority of the studies have concerned the amatoxins, followed by the phallotoxins and, distantly, the other peptides. The organization of this chapter proceeds from the whole organism level to the intraorganismal level, concluding with toxin action at the molecular level.
Nature alone is antique, and the oldest art a mushroom.
—Thomas Carlyle
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References
Amati P, Blasi F, Di Porzio U, Ricchio A, Trabone C (1975) Hamster α-amanitin-resistant RNA polymerase II able to transcribe polyoma virus genome in somatic cell hybrids. Proc Natl Acad Sci USA 72:753–757
Anderl J, Echner H, Faulstich H (2012) Chemical modification allows phallotoxins and amatoxins to be used as tools in cell biology. Beilstein J Org Chem 8:2072–2084. https://doi.org/10.3762/bjoc.8.233
Azzolin L, Antolini N, Calderan A, Ruzza P, Sciacovelli M, Marin O, Mammi S, Bernardi P, Rasola A (2011) Antamanide, a derivative of Amanita phalloides, is a novel inhibitor of the mitochondrial permeability transition pore. PLoS One 6:e16280. https://doi.org/10.1371/journal.pone.0016280
Barbanti-Brodano G, Derenzini M, Fiume L (1974) Toxic action of a phalloidin-albumin conjugate on cells with a high protein uptake. Nature 248:63–65
Bartolomei MS, Corden JL (1987) Localization of an α-amanitin resistance mutation in the gene encoding the largest subunit of mouse RNA polymerase II. Mol Cell Biol 7:586–594
Bartolomei MS, Corden JL (1995) Clustered α-amanitin resistance mutations in mouse. Mol Gen Genet 246:778–782
Ben-Zeev A, Becker Y (1977) Requirement of host cell RNA polymerase II in the replication of herpes simplex virus in α-amanitin-sensitive and –resistant cell lines. Virology 76:246–253
Bowman EA, Riddle DL, Kelly W (2011) Amino acid substitutions in the Caenorhabditis elegans RNA polymerase II large subunit AMA-1/RPB-1 that result in α-amanitin resistance and/or reduced function. G3 1:411–416. https://doi.org/10.1534/g3.111.000968
Brueckner F, Cramer P (2008) Structural basis of transcription inhibition by α-amanitin and implications for RNA polymerase II translocation. Nat Struct Mol Biol 15:811–818. https://doi.org/10.1038/nsmb.1458
Brueckner F, Armache KJ, Cheung A, Damsma GE, Kettenberger H, Lehmann E, Sydow J, Cramer P (2009) Structure-function studies of the RNA polymerase II elongation complex. Acta Crystallogr D Biol Crystallogr 65:112–120. https://doi.org/10.1107/S0907444908039875
Bryant RE, Adelberg EA, Magee PT (1977) Properties of an altered RNA polymerase I1 activity from an α-amanitin-resistant mouse cell line. Biochemistry 16:4237–4244
Bushnell DA, Cramer P, Kornberg RD (2002) Structural basis of transcription: α-amanitin-RNA polymerase II cocrystal at 2.8 Å resolution. Proc Natl Acad Sci USA 99:1218–1222. https://doi.org/10.1073/pnas.251664698
Cain AK, Nester EW (1973) Ribonucleic acid polymerase in Allomyces arbuscula. J Bacteriol 115:769–776
Chafin DR, Guo H, Price DH (1995) Action of α-amanitin during pyrophosphorolysis and elongation by RNA polymerase II. J Biol Chem 270:19114–19119. https://doi.org/10.1074/jbc.270.32.19114
Chan VL, Whitmore GF, Siminovitch L (1972) Mammalian cells with altered forms of RNA polymerase II. Proc Natl Acad Sci USA 69:3119–3123. https://doi.org/10.1073/pnas.69.11.3119
Chen Y, Weeks J, Mortin MA, Greenleaf AL (1993) Mapping mutations in genes encoding the two large subunits of Drosophila RNA polymerase II defines domains essential for basic transcription functions and for proper expression of developmental genes. Mol Cell Biol 13:4214–4222
Cheung ACM, Cramer P (2012) A movie of RNA polymerase II transcription. Cell 149:1431–1437. https://doi.org/10.1016/j.cell.2012.06.006. http://www.mpibpc.mpg.de/12602574/download and https://www.youtube.com/watch?v=WlMV_l88Lus
Cooper JA (1987) Effects of cytochalasin and phalloidin on actin. J Cell Biol 105:1473–1478
Coulter DE, Greenleaf AL (1982) Properties of mutationally altered RNA polymerases II of Drosophila. J Biol Chem 257:1945–1952
Coulter DE, Greenleaf AL (1985) A mutation in the largest subunit of RNA polymerase II alters RNA chain elongation in vitro. J Biol Chem 260:13190–13198
Delgado MA, Rintoul MR, Farías RN, Salomón RA (2001) Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J Bacteriol 183:4543–4550. https://doi.org/10.1128/JB.183.15.4543-4550.2001
Desjardins AE, Proctor RH (2007) Molecular biology of Fusarium mycotoxins. Int J Food Microbiol 119:47–50. https://doi.org/10.1016/j.ijfoodmicro.2007.07.024
Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P (2013) RNA polymerase I structure and transcription regulation. Nature 502:650–655. https://doi.org/10.1038/nature12712
Falcigno L, Costantini S, D’Auria G, Bruno BM, Zobeley S, Zanotti G, Paolillo L (2001) Phalloidin synthetic analogues: structural requirements in the interaction with F-actin. Chemistry 7:4665–4673
Faulstich H, Fiume L (1985) Protein conjugates of fungal toxins. Methods Enzymol 112:225–237
Faulstich H, Zilker TR (1994) Amatoxins. In: Spoerke DG, Rumack BH (eds) Handbook of mushroom poisoning: diagnosis and treatment. CRC Press, Boca Raton, pp 233–248
Faulstich H, Zobeley S, Rinnerthaler G, Small JV (1988) Fluorescent phallotoxins as probes for filamentous actin. J Muscle Res Cell Motil 9:370–383
Faulstich H, Zobeley S, Bentrup U, Jockusch BM (1989) Biotinylphallotoxins: preparation and use as actin probes. J Histochem Cytochem 37:1035–1045. https://doi.org/10.1177/37.7.2499619
Fehrenbach T, Cui Y, Faulstich H, Keppler D (2003) Characterization of the transport of the bicyclic peptide phalloidin by human hepatic transport proteins. Naunyn Schmiedeberg’s Arch Pharmacol 368:415–420. https://doi.org/10.1007/s00210-003-0814-4
Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW (2013) Crystal structure of the 14-subunit RNA polymerase I. Nature 502:644–649. https://doi.org/10.1038/nature12636
Fiume L, Barbanti-Brodano G (1974) Selective toxicity of amanitin-albumin conjugates for macrophages. Experientia 30:76–77. https://doi.org/10.1007/BF01921609
Frimmer M (1987) What we have learned from phalloidin. Toxicol Lett 35:169–182
Gavrilova O, Geyer J, Petzinger E (2007) In vivo relevance of Mrp2-mediated biliary excretion of the Amanita mushroom toxin demethylphalloin. Biochim Biophys Acta 1768:2070–2077. https://doi.org/10.1016/j.bbamem.2007.07.006
Giami S, Simchen G (1977) Incorporation of [3H]UMP into yeast spheroplasts in a hypotonic solution. Exp Cell Res 106:450–454
Gong XQ, Nedialkov YA, Burton ZF (2004) α-Amanitin blocks translocation by human RNA polymerase II. J Biol Chem 279:27422–27427. https://doi.org/10.1074/jbc.M402163200
Greenleaf AL (1983) Amanitin-resistant RNA polymerase II mutations are in the enzyme’s largest subunit. J Biol Chem 258:13403–13406
Greenleaf AL, Borsett LM, Jiamachello PF, Coulter DE (1979) α-Amanitin-resistant D. melanogaster with an altered RNA polymerase II. Cell 18:613–622. https://doi.org/10.1016/0092-8674(79)90116-8
Guialis A, Beatty BG, Ingles CJ, Crerar MM (1977) Regulation of RNA polymerase II activity in α-amanitin-resistant CHO hybrid cells. Cell 10:53–60. https://doi.org/10.1016/0092-8674(77)90139-8
Gundala S, Wells LD, Milliano MT, Talkad V, Luxon BA, Neuschwander-Tetri BA (2003) The hepatocellular bile acid transporter Ntcp facilitates uptake of the lethal mushroom toxin α-amanitin. Arch Toxicol 78:68–73. https://doi.org/10.1007/s00204-003-0527-y
Haag JR, Ream TS, Marasco M, Nicora CD, Norbeck AD, Paša-Tolić, Pikaard CS (2012) In vitro transcription activities of Pol IV, Pol V, and RDR2 reveal coupling of Pol IV and RDR2 for dsRNA synthesis in plant RNA silencing. Mol Cell 48:811–818. https://doi.org/10.1016/j.molcel.2012.09.027
Hager GL, Holland MJ, Rutter WJ (1977) Isolation of ribonucleic acid polymerases I, II, and III from Saccharomyces cerevisiae. Biochemistry 16:1–8
Hagenbuch B, Meier PJ (2004) Organic anion transporting polypeptides of the OATP/SLC21 family: phylogenetic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties. Pflugers Arch 447:653–665. https://doi.org/10.1007/s00424-003-1168-y
He L, Vasiliou K, Nebert DW (2009) Analysis and update of the human solute carrier (SLC) gene superfamily. Hum Genomics 3:195–206
Hendzel MJ (2014) The F-act’s of nuclear actin. Curr Opin Cell Biol 28:84–89. https://doi.org/10.1016/j.ceb.2014.04.003
Hoch HC, Staples RC (1983) Visualization of actin in situ by rhodamine-conjugated phalloin in the fungus Uromyces phaseoli. Eur J Cell Biol 32:52–58
Holtorf H, Schöb H, Kunz C, Waldvogel R, Meins F Jr (1999) Stochastic and nonstochastic post-transcriptional silencing of chitinase and β-1,3-glucanase genes involves increased RNA turnover – possible role for ribosome-independent RNA degradation. Plant Cell 11:471–483
Holzinger A, Blaas K (2016) Actin-dynamics in plant cells: the function of actin-perturbing substances: jasplakinolide, chondramides, phalloidin, cytochalasins, and latrunculins. Meth Mol Biol 1365:243–261. https://doi.org/10.1007/978-1-4939-3124-8_13
Horgen PA, Griffin DH (1971) Specific inhibitors of the three RNA polymerases from the aquatic fungus Blastocladiella emersonii. Proc Natl Acad Sci USA 68:338–341
Horgen PA, Vaisius AC, Ammirati JF (1978) The insensitivity of mushroom nuclear RNA polymerase activity to inhibition by amatoxins. Arch Microbiol 118:317–319
Ingles CJ (1978) Temperature-sensitive RNA polymerase II mutations in Chinese hamster ovary cells. Proc Natl Acad Sci USA 75:405–409
Izdebska M, Gagat M, Grzanka D, Grzanka A (2013) Ultrastructural localization of F-actin using phalloidin and quantum dots in HL-60 promyelocytic leukemia cell line after cell death induction by arsenic trioxide. Acta Histochem 115:487–495. https://doi.org/10.1016/j.acthis.2012.11.005
Jacob ST, Sajdel EM, Munro HN (1970) Specific action of α-amanitin on mammalian RNA polymerase protein. Nature 225:60–62
Jaenike J, Grimaldi DA, Sluder AE, Greenleaf AL (1983) α-Amanitin tolerance in mycophagous Drosophila. Science 221:165–167. https://doi.org/10.1126/science.221.4606.165
Johnson BC, Preston JF (1979) Unique amanitin resistance of RNA synthesis in isolated nuclei from Amanita species accumulating amanitins. Arch Microbiol 122:161–167
Johnson BC, Preston JF (1980) α-Amanitin-resistant RNA polymerase II from carpophores of Amanita species accumulating amatoxins. Biochim Biophys Acta 607:102–114
Kaplan CD, Larsson KM, Kornberg RD (2008) The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by α-amanitin. Mol Cell 30:547–556. https://doi.org/10.1016/j.molcel.2008.04.023
Kaster BC, Knippa KC, Kaplan CD, Peterson DO (2016) RNA polymerase II trigger loop mobility: indirect effects of Rpb9. J Biol Chem 291:14883–14895. https://doi.org/10.1074/jbc.M116.714394
Kaya E, Surmen MG, Yaykasli KO, Karahan S, Oktay M, Turan H, Colakoglu S, Erdem H (2014) Dermal absorption and toxicity of alpha amanitin in mice. Cutan Ocul Toxicol 33:154–160. https://doi.org/10.3109/15569527.2013.802697
Kedinger C, Gniazdowski M, Mandel JL, Gissinger F, Chambon P (1970) α-Amanitin: a specific inhibitor of one of the two DNA-dependent RNA polymerase activities from calf thymus. Biochem Biophys Res Commun 38:165–171
Klug A (2001) Structural biology: a marvellous machine for making messages. Science 292:1844–1846. https://doi.org/10.1126/science.1062384
Kramer W (2011) Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery. Biol Chem 392:77–94. https://doi.org/10.1515/BC.2011.017
Lachapelle M, Aldrich HC (1988) Phalloidin-gold complexes: a new tool for ultrastructural localization of F-actin. J Histochem Cytochem 36:1197–1202. https://doi.org/10.1177/36.9.3403970
Lengsfeld AM, Löw I, Wieland T, Dancker P, Hasselbach W (1974) Interaction of phalloidin with actin. Proc Natl Acad Sci USA 71:2803–2807
Letschert K, Faulstich H, Keller D, Keppler D (2006) Molecular characterization and inhibition of amanitin uptake into human hepatocytes. Toxicol Sci 91:140–149. https://doi.org/10.1093/toxsci/kfj141
Lindell TJ (1984) This week’s citation classic. Current contents no. 29, July 16, 1984. Accessed 5 Jul 2017 at: garfield.library.upenn.edu/classics1984/A1984SY56700002.pdf
Lindell TJ, Weinberg F, Morris PW, Roeder RG, Rutter WJ (1970) Specific inhibition of nuclear RNA polymerase II by α-amanitin. Science 170:447–449
Litten W (1975) The most poisonous mushrooms. Sci Am 232:90–101
Liu X, Qu X, Jiang Y, Chang M, Zhang R, Wu Y, Fu Y, Huang S (2015) Profilin regulates apical actin polymerization to control polarized pollen tube growth. Mol Plant 8:1694–1709. https://doi.org/10.1016/j.molp.2015.09.013
Lobban PE, Siminovitch L, Ingles CJ (1976) The RNA polymerase II of an α-amanitin-resistant Chinese hamster ovary cell line. Cell 8:65–70
Loros JJ, Dunlap JC (1991) Neurospora crassa clock-controlled genes are regulated at the level of transcription. Mol Cell Biol 11:558–563
Lovy-Wheeler A, Wilsen KL, Baskin TI, Hepler PK (2005) Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube. Planta 221:95–104. https://doi.org/10.1007/s00425-004-1423-2
Lu H, Choudhuri S, Ogura K, Csanaky IL, Lei X, Cheng X, Song PZ, Klaassen CD (2008) Characterization of organic anion transporting polypeptide 1b2-null mice: essential role in hepatic uptake/toxicity of phalloidin and microcystin-LR. Toxicol Sci 103:35–45. https://doi.org/10.1093/toxsci/kfn038
Lu J, Trnka MJ, Roh SH, Robinson PJ, Shiau C, Fujimori DG, Chiu W, Burlingame AL, Guan S (2015) Improved peak detection and deconvolution of native electrospray mass spectra from large protein complexes. J Am Soc Mass Spectrom 26:2141–2151. https://doi.org/10.1007/s13361-015-1235-6
Maksimov MO, Pan SJ, James Link A (2012) Lasso peptides: structure, function, biosynthesis, and engineering. Nat Prod Rep 29:996–1006. https://doi.org/10.1039/c2np20070h
Maunder JE, Voitk AJ (2010) What we don’t know about slugs and mushrooms. Fungi 3:36–44
Meier-Abt F, Faulstich H, Hagenbuch B (2004) Identification of phalloidin uptake systems of rat and human liver. Biochim Biophys Acta 1664:64–69. https://doi.org/10.1016/j.bbamem.2004.04.004
Militello KT, Patel V, Chessler AD, Fisher JK, Kasper JM, Gunasekera A, Wirth DF (2005) RNA polymerase II synthesizes antisense RNA in Plasmodium falciparum. RNA 11:365–370. https://doi.org/10.1261/rna.7940705
Montarolo PG, Goelet P, Castellucci VF, Morgan J, Kandel ER, Schacher S (1986) A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia. Science 234:1249–1254
Niedermeyer TH, Daily A, Swiatecka-Hagenbruch M, Moscow JA (2014) Selectivity and potency of microcystin congeners against OATP1B1 and OATP1B3 expressing cancer cells. PLoS One 10:e91476. https://doi.org/10.1371/journal.pone.0091476
Nielsen O (1986) Antamanide antagonizes phalloidin-induced human lymphocyte aggregation and prevents leukaemic mice from death: a pilot study. Acta Pharmacol Toxicol 59:249–251
Nothnagel EA, Barak LS, Sanger JW, Webb WW (1981) Fluorescence studies on modes of cytochalasin B and phallotoxin action on cytoplasmic streaming in Chara. J Cell Biol 88:364–372
Oda T, Namba K, Maéda Y (2005) Position and orientation of phalloidin in F-actin determined by X-ray fiber diffraction analysis. Biophys J 88:2727–2736. https://doi.org/10.1529/biophysj.104.047753
Opalski KS, Schultheiss H, Kogel KH, Huckelhoven R (2005) The receptor-like MLO protein and the RAC/ROP family G-protein RACB modulate actin reorganization in barley attacked by the biotrophic powdery mildew fungus Blumeria graminis f.sp. hordei. Plant J 41:291–303. https://doi.org/10.1111/j.1365-313X.2004.02292.x
Patturajan M (1995) Purification and characterization of DNA-dependent RNA polymerase II from Candida utilis. Biochem Mol Biol Int 37:295–304
Petryszak R, Keays M, Tang YA, Fonseca NA, Barrera E, Burdett T, Füllgrabe A, Fuentes AM, Jupp S, Koskinen S, Mannion O, Huerta L, Megy K, Snow C, Williams E, Barzine M, Hastings E, Weisser H, Wright J, Jaiswal P, Huber W, Choudhary J, Parkinson HE, Brazma A (2016) Expression atlas update – an integrated database of gene and protein expression in humans, animals, and plants. Nucl Acids Res 44:D746–D752. https://doi.org/10.1093/nar/gkv1045
Petzinger E, Burckhardt G, Schwenk M, Faulstich H (1982) Lack of intestinal transport of [3H]-demethylphalloin: comparative studies with phallotoxins and bile acids on isolated small intestinal cells and ileal brush border membrane vesicles. Naunyn Schmiedeberg’s Arch Pharmacol 320:196–200
Pulman JA, Childs KL, Sgambelluri RM, Walton JD (2016) Expansion and diversification of the MSDIN family of cyclic peptide genes in the poisonous agarics Amanita phalloides and A. bisporigera. BMC Genomics 17:1038. https://doi.org/10.1186/s12864-016-3378-7
Quon DV, Delgadillo MG, Johnson PJ (1996) Transcription in the early diverging eukaryote Trichomonas vaginalis: an unusual RNA polymerase II and α-amanitin-resistant transcription of protein-coding genes. J Mol Evol 43:253–262
Rödicker F, Ossenbühl F, Michels D, Benecke BJ (1999) Faithful in vitro transcription by fission yeas tRNA polymerase III reveals unique alpha-amanitin sensitivity. Gene Expr 8:165–174
Rogalski TM, Bullerjahn AME, Riddle DL (1988) Lethal and amanitin-resistance mutations in the Caenorhabditis elegans ama-1 and ama-2 genes. Genetics 120:409–422
Rogalski TM, Golomb M, Riddle DL (1990) Mutant Caenorhabditis elegans RNA polymerase II with a 20,000-fold reduced sensitivity to α-amanitin. Genetics 126:889–898
Rudd MD, Luse DS (1996) Amanitin greatly reduces the rate of transcription by RNA polymerase II ternary complexes but fails to inhibit some transcript cleavage modes. J Biol Chem 271:21549–21558
Ruzza P, Calderan A, Biondi B, Carrara M, Tancredi T, Borin G (1999) Ion-binding and pharmacological properties of Tyr6 and Tyr9 antamanide analogs. J Pep Res 53:442–452
Sainsbury S, Bernecky C, Cramer P (2015) Structural basis of transcription initiation by RNA polymerase II. Nat Rev Mol Cell Biol 16:129–143. https://doi.org/10.1038/nrm3952
Sanford T, Golomb M, Riddle DL (1983) RNA polymerase II from wild-type and amanitin-resistant strains of Caenorhabditis elegans. J Biol Chem 258:12804–12809
Schultz LD, Hall B (1976) Transcription in yeast: α-amanitin sensitivity and other properties which distinguish between RNA polymerases I and III. Proc Natl Acad Sci U S A 73:1029–1033
Seshadri V, McArthur AG, Sogin ML, Adam RD (2003) Giardia lamblia RNA polymerase II: amanitin-resistant transcription. J Biol Chem 278:27804–27810. https://doi.org/10.1074/jbc.M303316200
Siemion IZ, Pedyczak A, Trojnar J, Zimecki M, Wieczorek Z (1992) Immunosuppressive activity of antamanide and some of its analogues. Peptides 13:1233–1237
Skillman KM, Diraviyam K, Khan A, Tang K, Sept D, Sibley LD (2011) Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites. PLoS Pathog 7:e1002280. https://doi.org/10.1371/journal.ppat.1002280
Small J, Rottner K, Hahne P, Anderson KI (1999) Visualising the actin cytoskeleton. Microsc Res Tech 47:3–17. https://doi.org/10.1002/(SICI)1097-0029(19991001)47:1<3::AID-JEMT2>3.0.CO;2-2
Somers DG, Pearson ML, Ingles CJ (1975) Regulation of RNA polymerase II activity in a mutant rat myoblast cell line resistant to α-amanitin. Nature 253:372–374
Steeg CM, Ellis J, Bernstein A (1990) Introduction of specific point mutations into RNA polymerase II by gene targeting in mouse embryonic stem cells: evidence for a DNA mismatch repair mechanism. Proc Natl Acad Sci U S A 87:4680–4684
Steinmetz MO, Stoffler D, Müller SA, Jahn W, Wolpensinger B, Goldie KN, Engel A, Faulstich H, Aebi U (1998) Evaluating atomic models of F-actin with an undecagold-tagged phalloidin derivative. J Mol Biol 276:1–6. https://doi.org/10.1006/jmbi.1997.1529
Stirpe F, Fiume L (1967) Effect of α-amanitin on ribonucleic acid synthesis and on ribonucleic acid polymerase in mouse liver. Biochem J 103:67P–68P
Stunnenberg HG, Wennekes LM, Spierings T, van den Broek HW (1981) An α-amanitin-resistant DNA-dependent RNA polymerase II from the fungus Aspergillus nidulans. Eur J Biochem 117:121–129
Tellez de Iñon MT, Leoni PD, Torres HN (1974) RNA polymerase activities in Neurospora crassa. FEBS Lett 39:91–95
Thell K, Hellinger R, Schabbauer G, Gruber CW (2014) Immunosuppressive peptides and their therapeutic applications. Drug Discov Today 19:645–653. https://doi.org/10.1016/j.drudis.2013.12.002
Theologis A, Huynh TV, Davis RW (1985) Rapid induction of specific mRNAs by auxin in pea epicotyl tissue. J Mol Biol 183:53–68
Timberlake WE, Turian G (1974) Multiple DNA-dependent RNA polymerases of Neurospora. Experientia 30:1236–1238
Trauner M, Boyer JL (2003) Bile salt transporters: molecular characterization, function, and regulation. Physiol Rev 83:633–671. https://doi.org/10.1152/physrev.00027.2002
Tyler BM, Giles NH (1985) Accurate transcription of cloned Neurospora RNA polymerase II-dependent genes in vitro by homologous soluble extracts. Proc Natl Acad Sci U S A 82:5450–5454
Vaisius AC, Horgen PA (1979) Purification and characterization of RNA polymerase II resistant to α-amanitin from the mushroom Agaricus bisporus. Biochemistry 18:795–803
Van Gestel K, Le J, Verbelen JP (2001) A comparison of F-actin labeling methods for light microscopy in different plant specimens: multiple techniques supplement each other. Micron 32:571–578
Vaňáčová S, Tachezy J, Ullu E, Tschudi C (2001) Unusual diversity in α-amanitin sensitivity of RNA polymerases in trichomonads. Mol Biochem Parasitol 115:239–247
Vandekerckhove J, Deboben A, Nassal M, Wieland T (1985) The phalloidin binding site of F-actin. EMBO J 4:22815–22818
Verderame M, Alcorta D, Egnor M, Smith K, Pollack R (1980) Cytoskeletal F-actin patterns quantitated with fluorescein isothiocyanate-phalloidin in normal and transformed cells. Proc Natl Acad Sci USA 77:6624–6628
Von Olenhusen KG, Wohlfarth-Bottermann KE (1979) Evidence for actin transformation during the contraction-relaxation cycle of cytoplasmic actomyosin: cycle blockade by phalloidin injection. Cell Tissue Res 196:455–470
Walton JD (2000) Horizontal gene transfer and the evolution of secondary metabolite gene clusters in fungi: an hypothesis. Fung Genet Biol 30:167–171. https://doi.org/10.1006/fgbi.2000.1224
Wang D, Bushnell DA, Westover KD, Kaplan CD, Kornberg RD (2006) Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 127:941–954. https://doi.org/10.1016/j.cell.2006.11.023
Welbourn R, Goldman G, Kobzik L, Valeri CR, Hechtman HB, Shepro D (1985) Attenuation of IL-2-induced multisystem organ edema by phalloidin and antamanide. J Appl Physiol 70:1364–1368. https://doi.org/10.1152/jappl.1991.70.3.1364
Wieczorek Z, Siemion IZ, Zimecki M, Bolewska-Pedyczak E, Wieland T (1993) Immunosuppressive activity in the series of cycloamanide peptides from mushrooms. Peptides 14:1–5
Wieland T (1986) Peptides of poisonous Amanita mushrooms. Springer, New York
Wieland T, Faulstich H (1991) Fifty years of amanitin. Experientia 47:1186–1193
Wieland T, Götzendörfer C, Dabrowski J, Lipscomb WN, Shoham G (1983) Unexpected similarity of the structures of the weakly toxic amanitin (S)-sulfoxide and the highly toxic (R)-sulfoxide and sulfone as revealed by proton nuclear magnetic resonance and X-ray analysis. Biochemistry 22:1264–1271
Wulf E, Bautz L (1976) RNA polymerase B from an α-amanitin resistant mouse myeloma cell line. FEBS Lett 69:6–10
Wulf E, Deboben A, Bautz FA, Faulstich H, Wieland T (1979) Fluorescent phallotoxin, a tool for the visualization of cellular actin. Proc Natl Acad Sci USA 76:4498–4502
Xue JH, Wu P, Chi YL, Xu LX, Wei XY (2011) Cyclopeptides from Amanita exitialis. Nat Prod Bioprospect 1:52–66
Yanagida T, Nakase M, Nishiyama K, Oosawa F (1984) Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307:58–60
Young HA, Whiteley HR (1975) Deoxyribonucleic acid-dependent ribonucleic acid polymerases in the dimorphic fungus Mucor rouxii. J Biol Chem 250:479–487
Yu YP, Jackson SL, Garrill A (2004) Two distinct distributions of F-actin are present in the hyphal apex of the oomycete Achlya bisexualis. Plant Cell Physiol 45:275–280
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Walton, J. (2018). Biological Activities of the Amanita Peptide Toxins. In: The Cyclic Peptide Toxins of Amanita and Other Poisonous Mushrooms. Springer, Cham. https://doi.org/10.1007/978-3-319-76822-9_5
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Print ISBN: 978-3-319-76821-2
Online ISBN: 978-3-319-76822-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)