Abstract
Sulfur is necessary for the synthesis of cysteine. Microorganisms can use sulfate, thiosulfate or sulfonates as sole sulfur sources. These compounds are taken up by specific transporters followed by the conversion of sulfate or sulfonates into sulfide in 2 to 4 steps. The biosynthesis of cysteine from serine in bacteria is carried out by a two-step pathway beginning with the O-acetylation of serine, followed by O-re placement of the acetyl group by sulfide or thiosulfate. Some microorganisms can also use methionine or cysteine-derived compounds such as glutathione as sole sulfur source. Glutathione is degraded to liberate cysteine, whereas methionine is converted into cysteine via the reverse transsulfuration pathway or via methanethiol formation. Cysteine is also taken up directly from the environment by ABC transporters or symporters mainly as cystine, the disulfide-linked cysteine dimer. Several mechanisms are involved in the control of the intracellular concentration of cysteine, which is a highly reactive compound due to its –SH group. This amino acid is degraded mainly by cysteine desulfhydrases or is excreted by exporters. A large variety of molecular mechanisms participate in fine-tuning the regulation of cysteine metabolism: positive regulation by LysR-type regulators, negative control by repressors of the Rrf2 or TetR family and regulation by premature termination of transcription. In Escherichia coli and Bacillus subtilis, a global regulator, CysB and CymR, respectively, controls cysteine synthesis and transport in response to O-acetylserine or its derivative N-acetyl-serine availability. In Lactococcus lactis and Corynebacterium glutamicum, a unique regulator modulates the methionine and cysteine metabolisms. Cysteine or derivative compounds are biotechnically interesting. Fermentation processes with E. coli or C. glutamicum involving mutants insensitive to feedback inhibition by cysteine and also strains overproducing cysteine exporters or inactivated for cysteine degradative enzymes are currently being developed.
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References
Albanesi D, Mansilla MC, Schujman GE, de Mendoza D (2005) Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation. J Bacteriol 187:7631–7638
Amarita F, Yvon M, Nardi M, Chambellon E, Delettre J, Bonnarme P (2004) Identification and functional analysis of the gene encoding methionine-γ-lyase in Brevibacterium linens. Appl Environ Microbiol 70:7348–7354
Auger S, Danchin A, Martin-Verstraete I (2002) Global expression profile of Bacillus subtilis grown in the presence of sulfate or methionine. J Bacteriol 184:5179–5186
Auger S, Gomez MP, Danchin A, Martin-Verstraete I (2005) The PatB protein of Bacillus subtilis is a C–S-lyase. Biochimie 87:231–238
Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S (2003) Effect of cysteine desulfhydrase gene disruption on l-cysteine overproduction in Escherichia coli. Appl Microbiol Biotechnol 62:239–243
Awano N, Wada M, Mori H, Nakamori S, Takagi H (2005) Identification and functional analysis of Escherichia coli cysteine desulfhydrases. Appl Environ Microbiol 71:4149–4152
Baptist EW, Kredich NM (1977) Regulation of l-cystine transport in Salmonella typhimurium. J Bacteriol 131:111–118
Becker MA, Kredich NM, Tomkins GM (1969) The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J Biol Chem 244:2418–2427
Berger EA, Heppel LA (1972) A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J Biol Chem 247:7684–7694
Berndt C, Lillig CH, Wollenberg M, Bill E, Mansilla MC, de Mendoza D, Seidler A, Schwenn JD (2004) Characterization and reconstitution of a 4Fe–4S adenylyl sulfate/phosphoadenylyl sulfate reductase from Bacillus subtilis. J Biol Chem 279:7850–7855
Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T (2000) Identification of a new class of 5′-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria. J Bacteriol 182:135–142
Bonnarme P, Psoni L, Spinnler HE (2000) Diversity of l-methionine catabolism pathways in cheese-ripening bacteria. Appl Environ Microbiol 66:5514–5517
Bruinenberg PG, de Roo G, Limsowtin GK (1996) Purification and characterization of cystathionine γ-lyase from Lactococcus lactis subsp. cremoris SK11: possible role in flavor compound formation during cheese maturation. Appl Environ Microbiol 63:561–566
Burguiere P, Auger S, Hullo MF, Danchin A, Martin-Verstraete I (2004) Three different systems participate in l-cystine uptake in Bacillus subtilis. J Bacteriol 186:4875–4884
Burguière P, Fert J, Guillouard I, Auger S, Danchin A, Martin-Verstraete I (2005) Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism. J Bacteriol 187:6019–6030
Burns KE, Baumgart S, Dorrestein PC, Zhai HL, McLafferty FW, Begley TP (2005) Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis. J Am Chem Soc 127:11602–11603
Bykowski T, van der Ploeg JR, Iwanicka-Nowicka R, Hryniewicz MM (2002) The switch from inorganic to organic sulphur assimilation in Escherichia coli: adenosine 5′-phosphosulphate (APS) as a signalling molecule for sulphate excess. Mol Microbiol 43:1347–1358
Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A (2005) Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Protein Sci 14:2115–2124
Chang Z, Vining LC (2002) Biosynthesis of sulfur-containing amino acids in Streptomyces venezuelae ISP5230: roles for cystathionine β-synthase and transsulfuration. Microbiology 148:2135–2147
Chu L, Ebersole JL, Kurzban GP, Holt SC (1997) Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities. Infect Immun 65:3231–3238
Dassler T, Maier T, Winterhalter C, Bock A (2000) Identification of a major facilitator protein from Escherichia coli involved in efflux of metabolites of the cysteine pathway. Mol Microbiol 36:1101–1112
Denk D, Bock A (1987) l-cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant. J Gen Microbiol 133:515–525
During-Olsen L, Regenberg B, Gjermansen C, Kielland-Brandt MC, Hansen J (1999) Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases. Curr Genet 35:609–617
Even S, Burguière P, Auger S, Soutourina O, Danchin A, Martin-Verstraete I (2006) Global control of cysteine metabolism by CymR in Bacillus subtilis. J Bacteriol 188:2184–2197
Franke I, Resch A, Dassler T, Maier T, Bock A (2003) YfiK from Escherichia coli promotes export of O-acetylserine and cysteine. J Bacteriol 185:1161–1166
Fukamachi H, Nakano Y, Yoshimura M, Koga T (2002) Cloning and characterization of the l-cysteine desulfhydrase gene of Fusobacterium nucleatum. FEMS Microbiol Lett 215:75–80
Gagnon Y, Breton R, Putzer H, Pelchat M, Grunberg-Manago M, Lapointe J (1994) Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis. J Biol Chem 269:7473–7482
Golic N, Schliekelmann M, Fernandez M, Kleerebezem M, van Kranenburg R (2005) Molecular characterization of the CmbR activator-binding site in the metC-cysK promoter region in Lactococcus lactis. Microbiology 151:439–446
Guillouard I, Auger S, Hullo MF, Chetouani F, Danchin A, Martin-Verstraete I (2002) Identification of Bacillus subtilis CysL, a regulator of the cysJI operon, which encodes sulfite reductase. J Bacteriol 184:4681–4689
Haitani Y, Awano N, Yamazaki M, Wada M, Nakamori S, Takagi H (2006) Functional analysis of l-serine O-acetyltransferase from Corynebacterium glutamicum. FEMS Microbiol Lett 255:156–163
Hindson VJ (2003) Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine. Biochem J 375:745–752
Hosie AHF, Poole PS (2001) Bacterial ABC transporters of amino acids. Res Microbiol 152:259–270
Hryniewicz MM, Kredich NM (1991) The cysP promoter of Salmonella typhimurium: characterization of two binding sites for CysB protein, studies of in vivo transcription initiation, and demonstration of the anti-inducer effects of thiosulfate. J Bacteriol 173:5876–5886
Huang B, Vetting MW, Roderick SL (2005) The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. J Bacteriol 187:3201–3205
Hulanicka MD, Hallquist SG, Kredich NM, Mojica AT (1979) Regulation of O-acetylserine sulfhydrylase B by l-cysteine in Salmonella typhimurium. J Bacteriol 140:141–146
Hung J, Turner MS, Walsh T, Giffard PM (2005) BspA (CyuC) in Lactobacillus fermentum BR11 is a highly expressed high-affinity l-cystine-binding protein. Curr Microbiol 50:33–37
Inoue H, Inagaki K, Eriguchi SI, Tamura T, Esaki N, Soda K, Tanaka H (1997) Molecular characterization of the mde operon involved in l-methionine catabolism of Pseudomonas putida. J Bacteriol 179:3956–3962
Iwanicka-Nowicka R, Hryniewicz MM (1995) A new gene, cbl, encoding a member of the LysR family of transcriptional regulators belongs to Escherichia coli cys regulon. Gene 166:11–17
Johansson P, Hederstedt L (1999) Organization of genes for tetrapyrrole biosynthesis in gram-positive bacteria. Microbiology 145:529–538
Johnson CM, Huang B, Roderick SL, Cook PF (2004) Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Arch Biochem Biophys 429:115–122
Kari C, Nagy Z, Kovacs P, Hernadi F (1971) Mechanism of the growth inhibitory effect of cysteine on Escherichia coli. J Gen Microbiol 68:349–356
Kawashima CG, Berkowitz O, Hell R, Noji M, Saito K (2005) Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis. Plant Physiol 137:220–230
Kertesz MA (2001) Bacterial transporters for sulfate and organosulfur compounds. Res Microbiol 152:279–290
Kertesz MA, Wietek C (2001) Desulfurization and desulfonation: applications of sulfur-controlled gene expression in bacteria. Appl Microbiol Biotechnol 57:460–466
Koch DJ, Ruckert C, Albersmeier A, Huser AT, Tauch A, Puhler A, Kalinowski J (2005a) The transcriptional regulator SsuR activates expression of the Corynebacterium glutamicum sulphonate utilization genes in the absence of sulphate. Mol Microbiol 58:480–494
Koch DJ, Ruckert C, Rey DA, Mix A, Puhler A, Kalinowski J (2005b) Role of the ssu and seu genes of Corynebacterium glutamicum ATCC 13032 in utilization of sulfonates and sulfonate esters as sulfur sources. Appl Environ Microbiol 71:6104–6114
Kredich NM (1996) Biosynthesis of Cysteine. In: Neidhardt FC (ed) Escherichia coli and Salmonella, cellular and molecular biology. ASM Press, Washington DC, p 514–527
Lai CY, Baumann P (1992) Sequence analysis of a DNA fragment from Buchnera aphidicola (an endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE, and secB. Gene 119:113–118
Leuchtenberger W, Huthmacher K, Drauz K (2005) Biotechnical production of amino acids and derivatives: current status and prospects. Appl Microbiol Biotechnol 69:1–8
Lillig CH, Prior A, Schwenn JD, Aslund F, Ritz D, Vlamis-Gardikas A, Holmgren A (1999) New thioredoxins and glutaredoxins as electron donors of 3′-phosphoadenylylsulfate reductase. J Biol Chem 274:7695–7698
Lithgow JK, Hayhurst EJ, Cohen G, Aharonowitz Y, Foster SJ (2004) Role of a cysteine synthase in Staphylococcus aureus. J Bacteriol 186:1579–1590
Lochowska A, Iwanicka-Nowicka R, Zaim J, Witkowska-Zimny M, Bolewska K, Hryniewicz MM (2004) Identification of activating region (AR) of Escherichia coli LysR-type transcription factor CysB and CysB contact site on RNA polymerase alpha subunit at the cysP promoter. Mol Microbiol 53:791–806
Maier THP (2003) Semisynthetic production of unnatural l-α-aminoacids by metabolic engineering of the cysteine biosynthetic pathway. Nat Biotechnol 21:422–427
Mansilla MC, Albanesi D, de Mendoza D (2000) Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in l-cysteine biosynthesis in Bacillus subtilis. J Bacteriol 182:5885–5892
Mansilla MC, de Mendoza D (1997) l-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase. J Bacteriol 179:976–981
Mansilla MC, de Mendoza D (2000) The Bacillus subtilis cysP gene encodes a novel sulphate permease related to the inorganic phosphate transporter (Pit) family. Microbiology 146:815–821
Mendoza-Cozatl D, Loza-Tavera H, Hernandez-Navarro A, Moreno-Sanchez R (2005) Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiol Rev 29:653–671
Minami H, Suzuki H, Kumagai H (2003) A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity. FEMS Microbiol Lett 224:169–173
Mino K, Ishikawa K (2003a) Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J Bacteriol 185:2277–2284
Mino K, Ishikawa K (2003b) A novel O-phospho-l-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1. FEBS Lett 551:133–138
Muller A, Thomas GH, Horler R, Brannigan JA, Blagova E, Levdikov VM, Fogg MJ, Wilson KS, Wilkinson AJ (2005) An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein. Mol Microbiol 57:143–155
Nakamori S, Kobayashi SI, Kobayashi C, Takagi H (1998) Overproduction of l-cysteine and l-cystine by Escherichia coli strains with a genetically altered serine acetyltransferase. Appl Environ Microbiol 64:1607–1611
Nakamura T, Iwahashi H, Eguchi Y (1984) Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium. J Bacteriol 158:1122–1127
Oppezzo OJ (1998) In vivo effects of anti-inducers of the cysteine regulon in Salmonella typhimurium. FEMS Microbiol Lett 163:143–148
Ostrowski J, Kredich NM (1989) Molecular characterization of the cysJIH promoters of Salmonella typhimurium and Escherichia coli: regulation by cysB protein and N-acetyl-l-serine. J Bacteriol 171:130–140
Parry J, Clark DP (2002) Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli. FEMS Microbiol Lett 209:81–85
Pinto R, Tang QX, Britton WJ, Leyh TS, Triccas JA (2004) The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex. Microbiology 150:1681–1686
Pittman MS, Corker H, Wu G, Binet MB, Moir AJ, Poole RK (2002) Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly. J Biol Chem 277:49841–49849
Quadroni M, Staudenmann W, Kertesz M, James P (1996) Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli. Eur J Biochem 239:773–781
Rey DA, Nentwich SS, Koch DJ, Ruckert C, Puhler A, Tauch A, Kalinowski J (2005) The McbR repressor modulated by the effector substance S-adenosylhomocysteine controls directly the transcription of a regulon involved in sulphur metabolism of Corynebacterium glutamicum ATCC 13032. Mol Microbiol 56:871–887
Rey DA, Puhler A, Kalinowski J (2003) The putative transcriptional repressor McbR, member of the TetR-family, is involved in the regulation of the metabolic network directing the synthesis of sulfur containing amino acids in Corynebacterium glutamicum. J Biotechnol 103:51–65
Rodionov DA, Vitreschak AG, Mironov AA, Gelfand MS (2004) Comparative genomics of the methionine metabolism in Gram-positive bacteria: a variety of regulatory systems. Nucleic Acids Res 32:3340–3353
Ruckert C, Koch DJ, Rey DA, Albersmeier A, Mormann S, Puhler A, Kalinowski J (2005) Functional genomics and expression analysis of the Corynebacterium glutamicum fpr2-cysIXHDNYZ gene cluster involved in assimilatory sulphate reduction. BMC Genomics 6:121
Savijoki K, Ingmer H, Varmanen P (2006) Proteolytic systems of lactic acid bacteria. Appl Microbiol Biotechnol 71:394–406
Seiflein TA, Lawrence JG (2001) Methionine-to-cysteine recycling in Klebsiella aerogenes. J Bacteriol 183:336–346
Sekowska A, Danchin A (1999) Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis. DNA Res 6:255–264
Sirko A, Zatyka M, Sadowy E, Hulanicka D (1995) Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J Bacteriol 177:4134–4136
Sperandio B, Polard P, Ehrlich DS, Renault P, Guedon E (2005) Sulfur amino acid metabolism and its control in Lactococcus lactis IL1403. J Bacteriol 187:3762–3778
Suzuki H, Hashimoto W, Kumagai H (1993) Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. J Bacteriol 175:6038–6040
Suzuki H, Kamatani S, Kim ES, Kumagai H (2001) Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12. J Bacteriol 183:1489–1490
Suzuki H, Koyanagi T, Izuka S, Onishi A, Kumagai H (2005) The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J Bacteriol 187:5861–5867
Takagi H, Yoshioka K, Awano N, Nakamori S, Ono B (2003) Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis. FEMS Microbiol Lett 218:291–297
Thomas D, Surdin-Kerjan Y (1997) Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 61:503–532
Turner MS, Woodberry T, Hafner LM, Giffard PM (1999) The bspA locus of Lactobacillus fermentum BR11 encodes an l-cystine uptake system. J Bacteriol 181:2192–2198
van der Ploeg JR, Barone M, Leisinger T (2001a) Functional analysis of the Bacillus subtilis cysK and cysJI genes. FEMS Microbiol Lett 201:29–35
van der Ploeg JR, Cummings NJ, Leisinger T, Connerton IF (1998) Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates. Microbiology 144:2555–2561
van der Ploeg JR, Eichhorn E, Leisinger T (2001b) Sulfonate-sulfur metabolism and its regulation in Escherichia coli. Arch Microbiol 176:1–8
Vendeville A, Winzer K, Heurlier K, Tang CM, Hardie KR (2005) Making sense of metabolism: Autoinducer-2, LuxS and pathogenic bacteria. Nat Rev Microbiol 3:383–396
Vermeij P, Kertesz MA (1999) Pathways of assimilative sulfur metabolism in Pseudomonas putida. J Bacteriol 181:5833–5837
Wada M, Awano N, Haisa K, Takagi H, Nakamori S (2002) Purification, characterization and identification of cysteine desulfhydrase of Corynebacterium glutamicum, and its relationship to cysteine production. FEMS Microbiol Lett 217:103–107
Wheeler PR, Coldham NG, Keating L, Gordon SV, Wooff EE, Parish T, Hewinson RG (2005) Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic mycobacteria. J Biol Chem 280:8069–8078
White RH (2003) The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii. Biochim Biophys Acta 1624:46–53
Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR (2002) 5′-Adenosylphosphosulfate lies at a metabolic branchpoint in Mycobacteria. J Biol Chem 277:32606–32615
Wirtz M, Hell R (2006) Functional analysis of the cysteine synthase protein complex from plants: structural, biochemical and regulatory properties. J Plant Physiol 163:273–286
Wooff E, Michell SL, Gordon SV, Chambers MA, Bardarov S, Jacobs WR Jr, Hewinson RG, Wheeler PR (2002) Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Mol Microbiol 43:653–663
Yamagata S, D'Andrea RJ, Fujisaki S, Isaji M, Nakamura K (1993) Cloning and bacterial expression of the CYS3 gene encoding cystathionine γ-lyase of Saccharomyces cerevisiae and the physicochemical and enzymatic properties of the protein. J Bacteriol 175:4800–4808
Yoshida Y, Negishi M, Amano A, Oho T, Nakano Y (2003) Differences in the βC–S lyase activities of viridans group streptococci. Biochem Biophys Res Commun 300:55–60
Yvon M, Chambellon E, Bolotin A, Roudot-Algaron F (2000) Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763. Appl Environ Microbiol 66:571–577
Zhao C, Moriga Y, Feng B, Kumada Y, Imanaka H, Imamura K, Nakanishi K (2006) On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli. Biochem Biophys Res Commun 341:911–916
Zhao CH, Ohno K, Sogoh K, Imamura K, Sakiyama T, Nakanishi K (2004) Production of nonproteinaceous amino acids using recombinant Escherichia coli cells expressing cysteine synthase and related enzymes with or without the secretion of O-acetyl-l-serine. J Biosci Bioeng 97:322–328
Acknowledgments
We thank Pierre Burguière and Brice Sperandio whose PhD theses have been extremely helpful for the writing of this paper. We are grateful to Sandrine Auger and Olga Soutourina for critical reading of the paper. This research was supported by grants from the “Ministère de l'Education Nationale de la Recherche et de la Technologie”, the “Institut National de la Recherche argronomique” (UR895), the “Centre National de la Recherche Scientifique” (URA 2171), the “Institut Pasteur” and the “Université Paris 7”.
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Guédon, E., Martin-Verstraete, I. (2006). Cysteine Metabolism and Its Regulation in Bacteria. In: Wendisch, V.F. (eds) Amino Acid Biosynthesis ~ Pathways, Regulation and Metabolic Engineering. Microbiology Monographs, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/7171_2006_060
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