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Riding the sulfur cycle–metabolism of sulfonates and sulfate esters in Gram-negative bacteria

Kertesz, Michael A.·2000·FEMS Microbiology Reviews
DOI 10.1016/s0168-6445(99)00033-9
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  1. 10.1016/0143-148X(82)90042-8 · DOI
  2. 10.1146/annurev.nu.06.070186.001143 · DOI
  3. 10.1007/s004250050112 · DOI
  4. 10.1034/j.1399-3054.1996.970228.x · DOI
  5. Kredich, N.M. (1996) Biosynthesis of cysteine. In: Escherichia coli and Salmonella, 2nd edn. (Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. and Umbarger, H.E., Eds.), pp. 514–527, ASM Press, Washington, DC.
  6. Neidhardt F.C. Bloch P.L. Smith D.F. (1974) Culture medium for Enterobacteria. J. Bacteriol. 119, 736–747. · DOI
  7. 10.1111/j.1574-6976.1998.tb00378.x · DOI
  8. 10.1080/01490459809378070 · DOI
  9. 10.1146/annurev.micro.51.1.73 · DOI
  10. 10.1002/(SICI)1097-0061(19960915)12:11<1153::AID-YEA16>3.0.CO;2-2 · DOI
  11. Beil S. Kehrli H. James P. Staudenmann W. Cook A.M. Leisinger T. Kertesz M.A. (1995) Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA). Eur. J. Biochem. 229, 385–394. · DOI
  12. 10.1074/jbc.272.37.23031 · DOI · Paper page
  13. 10.1074/jbc.273.40.25560 · DOI
  14. Kertesz M.A. Schmidt K. Wüest T. (1999) A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa . J. Bacteriol. 181, 1464–1473. · DOI
  15. 10.1038/nbt1296-1705 · DOI
  16. Cerbelaud E.C. Conway L.J. Galliher P.M. Langer R.S. Cooney C.L. (1986) Sulfur regulation of heparinase and sulfatases in Flavobacterium heparinum . Appl. Environ. Microbiol. 51, 640–646. · DOI
  17. 10.1111/j.1365-2958.1992.tb01453.x · DOI
  18. 10.1046/j.1365-2958.1998.01105.x · DOI
  19. 10.1099/13500872-141-2-431 · DOI
  20. 10.1099/00221287-144-5-1375 · DOI
  21. Kertesz M.A. Leisinger T. Cook A.M. (1993) Proteins induced by sulfate limitation in Escherichia coli, Pseudomonas putida, or Staphylococcus aureus . J. Bacteriol. 175, 1187–1190. · DOI
  22. 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. · DOI
  23. 10.1002/elps.1150180318 · DOI
  24. Quadroni, M., James, P., Dainese-Hatt, P. and Kertesz, M.A. (1999) Proteome mapping, mass spectrometric sequencing and reverse transcriptase-PCR for characterisation of the sulfate starvation-induced response in Pseudomonas aeruginosa PAO1. Eur. J. Biochem. in press. · DOI
  25. Wanner, B.L. (1996) Phosphorus assimilation and control of the phosphate regulon. In: Escherichia coli and Salmonella, 2nd edn. (Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. and Umbarger, H.E., Eds.), pp. 1357–1381, ASM Press, Washington, DC.
  26. Jiang W.H. Metcalf W.W. Lee K.S. Wanner B.L. (1995) Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2. J. Bacteriol. 177, 6411–6421. · DOI
  27. 10.1046/j.1365-2958.1996.421953.x · DOI
  28. 10.1007/BF00330857 · DOI
  29. 10.1038/341245a0 · DOI
  30. 10.1016/S0065-2660(08)60398-3 · DOI
  31. 10.1146/annurev.mi.47.100193.000335 · DOI
  32. 10.1007/BF00331273 · DOI
  33. Hallmann A. Sumper M. (1994) An inducible arylsulfatase of Volvox carteri with properties suitable for a reporter-gene system: Purification, characterization and molecular cloning. Eur. J. Biochem. 221, 143–150. · DOI
  34. Dodgson, K.S., White, G.F. and Fitzgerald, J.W. (1982) Sulfatases of Microbial Origin. CRC Press, Boca Raton, FL.
  35. 10.1139/x86-124 · DOI
  36. Zehnder, A.J.B. and Zinder, S.H. (1980) The sulfur cycle. In: The Handbook of Environmental Chemistry (Hutzinger, O., Ed.), Vol. 1A, pp. 105–145, Springer, Berlin. · DOI
  37. 10.1021/bi00344a027 · DOI
  38. 10.1038/350627a0 · DOI
  39. 10.1146/annurev.arplant.49.1.53 · DOI
  40. Herbert, R.B., Holliman, F.G. Aeruginosin B – a naturally occurring phenazinesulphonic acid,. Proc. Chem. Soc. 1964, 1964. 19 · DOI
  41. 10.1021/ef960212a · DOI
  42. 10.1016/0016-7037(94)90200-3 · DOI
  43. Visscher P.T. Gritzer R.F. Leadbetter E.R. (1999) Low-molecular-weight sulfonates, a major substrate for sulfate reducers in marine microbial mats. Appl. Environ. Microbiol. 65, 3272–3278. · DOI
  44. 10.1021/es00048a012 · DOI
  45. 10.1029/92GL01995 · DOI
  46. 10.1016/0038-0717(93)90178-E · DOI
  47. 10.1016/0038-0717(93)90131-T · DOI
  48. Stevenson, F.J. (1994) Humus Chemistry: Genesis, Composition, Reactions, 2nd edn., Wiley, New York.
  49. 10.1080/10408419891294208 · DOI
  50. 10.1016/S0045-6535(97)00308-1 · DOI
  51. 10.1007/BF00322890 · DOI
  52. 10.1016/0045-6535(94)90064-7 · DOI
  53. 10.1002/etc.5620120908 · DOI
  54. 10.1016/S0045-6535(97)10021-2 · DOI
  55. Ainsworth S.J. (1996) Soaps and detergents. Chem. Eng. News 74 (4), 32–54. · DOI
  56. Holmstrup M. Krogh P.H. (1996) Effects of an anionic surfactant, linear alkylbenzene sulfonate, on survival, reproduction and growth of the soil-living collembolan Folsomia fimetaria . Environ. Toxicol. Chem. 15, 1745–1748. · DOI
  57. 10.1007/s002270050129 · DOI
  58. Utsunomiya A. Watanuki T. Matsushita K. Tomita I. (1997) Toxic effects of linear alkylbenzene sulfonate, quaternary alkylammonium chloride and their complexes on Dunaliella sp. and Chlorella pyrenoidosa . Environ. Toxicol. Chem. 16, 1247–1254. · DOI
  59. 10.1016/0043-1354(95)00143-9 · DOI
  60. 10.1021/es950210p · DOI
  61. 10.1021/es9803456 · DOI
  62. 10.1002/etc.5620120604 · DOI
  63. Nicholls, R.G. and Roy, A.B. (1971) Arylsulfatases. In: The Enzymes (Boyer, P.D., Ed.), Vol. 5, pp. 21–41, Academic, New York. · DOI
  64. 10.1177/096032719601500701 · DOI
  65. 10.1016/S0009-2797(97)00117-8 · DOI
  66. 10.1248/bpb.17.1326 · DOI
  67. 10.1016/0009-2797(94)90068-X · DOI
  68. 10.1073/pnas.95.6.2896 · DOI
  69. 10.1074/jbc.272.35.21700 · DOI
  70. 10.1146/annurev.ph.50.030188.002051 · DOI
  71. 10.3109/10409239509083490 · DOI
  72. Freeman, C. and Hopwood, J. (1992) Lysosomal degradation of heparin and heparan sulfate. In: Heparin and Related Polysaccharides (Lane, D.A., Björk, I. and Lindahl, U., Eds.), pp. 121–134, Plenum Press, New York. · DOI
  73. 10.1016/S0959-437X(97)80153-0 · DOI
  74. Painter, H.A. (1992) Anionic surfactants. In: The Handbook of Environmental Chemistry (Hutzinger, O., Ed.), Vol. 3F, pp. 1–88, Springer, Berlin. · DOI
  75. 10.1016/0043-1354(95)00082-V · DOI
  76. 10.1016/0143-1471(85)90020-0 · DOI
  77. 10.1083/jcb.106.1.29 · DOI
  78. 10.1099/13500872-141-11-2897 · DOI
  79. 10.1016/0012-1606(80)90436-4 · DOI
  80. Yamada K. Akasaka K. Shimada H. (1989) Structure of sea-urchin arylsulfatase gene. Eur. J. Biochem. 186, 405–410. · DOI
  81. 10.1016/0038-0717(90)90045-2 · DOI
  82. 10.1177/14.12.932 · DOI
  83. 10.1080/00103628009367094 · DOI
  84. 10.1007/BF00335931 · DOI
  85. 10.1016/0038-0717(75)90041-3 · DOI
  86. 10.1016/S0038-0717(97)00056-4 · DOI
  87. 10.1016/0038-0717(95)00032-A · DOI
  88. 10.1002/(SICI)1521-1878(199806)20:6<505::AID-BIES9>3.0.CO;2-K · DOI
  89. 10.1016/0092-8674(95)90314-3 · DOI
  90. 10.1074/jbc.273.9.4835 · DOI
  91. Murooka Y. Ishibashi K. Yasumoto M. Sasaki M. Sugino H. Azakami H. Yamashita M. (1990) A sulfur- and tyramine-regulated Klebsiella aerogenes operon containing the arylsulfatase (atsA) gene and the atsB gene. J. Bacteriol. 172, 2131–2140. · DOI
  92. Adachi T. Murooka Y. Harada T. (1975) Regulation of arylsulfatase synthesis by sulfur compounds in Klebsiella aerogenes . J. Bacteriol. 121, 29–35. · DOI
  93. Murooka Y. Harada T. (1981) Regulation of derepressed synthesis of arylsulfatase by tyramine oxidase in Salmonella typhimurium . J. Bacteriol. 145, 796–802. · DOI
  94. Henderson M.J. Milazzo F.H. (1979) Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis. J. Bacteriol. 139, 80–87. · DOI
  95. 10.1021/bi00890a014 · DOI
  96. 10.1139/m70-186 · DOI
  97. 10.1139/m72-089 · DOI
  98. 10.1111/j.1574-6968.1977.tb00944.x · DOI
  99. 10.1016/0020-711X(75)90090-7 · DOI
  100. Delisle G. Milazzo F.H. (1970) The isolation of arylsulphatase isoenzymes from Pseudomonas aeruginosa . Biochim. Biophys. Acta 212, 505–508. · DOI
  101. Adachi T. Murooka Y. Harada T. (1973) Derepression of arylsulfatase synthesis in Aerobacter aerogenes by tyramine. J. Bacteriol. 116, 19–24. · DOI
  102. 10.1042/bj0930373 · DOI
  103. 10.1099/00207713-40-1-66 · DOI
  104. 10.1099/00207713-42-2-315 · DOI
  105. 10.1074/jbc.274.22.15375 · DOI
  106. 10.1271/bbb1961.40.2071 · DOI
  107. 10.1099/00221287-13-3-572 · DOI
  108. 10.1073/pnas.94.22.11963 · DOI
  109. 10.1021/bi9810205 · DOI
  110. 10.1016/S0014-5793(98)00065-9 · DOI
  111. Selmer T. Hallmann A. Schmidt B. Sumper M. Figura K.V. (1996) The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri . Eur. J. Biochem. 238, 341–345. · DOI
  112. 10.1021/bi9714924 · DOI
  113. 10.1016/S0969-2126(97)00185-8 · DOI
  114. 10.1016/S1074-5521(98)90154-5 · DOI
  115. Flachmann R. Kunz N. Seifert J. Gutlich M. Wientjes F.J. Laufer A. Gassen H.G. (1988) Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB . Eur. J. Biochem. 175, 221–228. · DOI
  116. Kahnert, A., Vermeij, P., James, P., Leisinger, T. and Kertesz, M.A. (1999) The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313. Submitted for publication. · DOI
  117. 10.1074/jbc.271.42.25754 · DOI
  118. 10.1093/emboj/18.8.2084 · DOI
  119. 10.1271/bbb.60.935 · DOI
  120. 10.1046/j.1365-2958.1998.00764.x · DOI
  121. 10.1146/annurev.cellbio.8.1.67 · DOI
  122. 10.1038/346362a0 · DOI
  123. Walker J.E. Saraste M. Runswick M.J. Gay N.J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945–951. · DOI · Paper page
  124. Kawasaki S. Arai H. Kodama T. Igarashi Y. (1997) Gene cluster for dissimilatory nitrite reductase (nir) from Pseudomonas aeruginosa: Sequencing and identification of a locus for heme d-1 biosynthesis. J. Bacteriol. 179, 235–242. · DOI
  125. 10.1093/dnares/3.3.109 · DOI · Paper page
  126. 10.1093/nar/25.17.3389 · DOI · Paper page
  127. 10.1126/science.277.5331.1453 · DOI
  128. 10.1016/0003-9861(72)90385-2 · DOI
  129. 10.1002/jobm.3630190610 · DOI
  130. Yamashita M. Azakami H. Yokoro N. Roh J.H. Suzuki H. Kumagai H. Murooka Y. (1996) maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli . J. Bacteriol. 178, 2941–2947. · DOI
  131. 10.1271/bbb1961.48.1459 · DOI
  132. Azakami H. Murooka H.S. (1992) Cloning and nucleotide sequence of a negative regulator gene for Klebsiella aerogenes arylsulfatase synthesis and identification of the gene as folA . J. Bacteriol. 174, 2344–2351. · DOI
  133. 10.1042/bj3040937 · DOI
  134. 10.1023/A:1008883915003 · DOI
  135. Imperato T.J. Wong C.G. Chen L.J. Bolt R.J. (1977) Hydrolysis of lithocholate sulfate by Pseudomonas aeruginosa . J. Bacteriol. 130, 545–547. · DOI
  136. 10.1111/j.1574-6968.1987.tb02020.x · DOI
  137. 10.1007/BF00119760 · DOI
  138. 10.1099/00221287-139-12-2915 · DOI
  139. Higgins T.P. Hewlins M.J.E. White G.F. (1996) A C-13-NMR study of the mechanism of bacterial metabolism of monomethyl sulfate. Eur. J. Biochem. 236, 620–625. · DOI
  140. 10.1099/00221287-134-5-1229 · DOI
  141. 10.1073/pnas.95.19.11394 · DOI
  142. 10.1271/bbb.58.889 · DOI
  143. 10.1038/207385a0 · DOI
  144. 10.1016/0378-1119(92)90702-Q · DOI
  145. 10.1271/bbb.62.1739 · DOI
  146. Roberton A.M. Wright D.P. (1997) Bacterial glycosulphatases and sulphomucin degradation. Can. J. Gastroenterol. 11, 361–366. · DOI
  147. 10.1111/j.1472-765X.1991.tb00580.x · DOI
  148. 10.1099/00222615-48-6-551 · DOI
  149. 10.1016/S0968-0004(98)01264-X · DOI
  150. Salyers A.A. Kotarski S.F. (1980) Induction of chondroitin sulfate lyase activity in Bacteroides thetaiotaomicron . J. Bacteriol. 143, 781–788. · DOI
  151. Hwa V. Salyers A.A. (1992) Evidence for differential regulation of genes in the chondroitin sulfate utilization pathway of Bacteroides thetaiotaomicron . J. Bacteriol. 174, 342–344. · DOI
  152. Sugahara K. Kojima T. (1996) Specificity studies of bacterial sulfatases by means of structurally defined sulfated oligosaccharides isolated from shark cartilage chondroitin sulfate D. Eur. J. Biochem. 239, 865–870. · DOI
  153. Bruce J.S. McLean M.W. Williamson F.B. Long W.F. (1985) Flavobacterium heparinum 6-O-sulphatase for N-substituted glucosamine 6-O-sulphate. Eur. J. Biochem. 152, 75–82. · DOI
  154. Bruce J.S. McLean M.W. Long W.F. Williamson F.B. (1985) Flavobacterium heparinum 3-O-sulphatase for N-substituted glucosamine 3-O-sulphate. Eur. J. Biochem. 148, 359–365. · DOI
  155. McLean M.W. Bruce J.S. Long W.F. Williamson F.B. (1984) Flavobacterium heparinum 2-O-sulphatase for 2-O-sulphato-delta 4, 5-glycuronate-terminated oligosaccharides from heparin. Eur. J. Biochem. 145, 607–615. · DOI
  156. Bruce J.S. McLean M.W. Long W.F. Williamson F.B. (1987) Flavobacterium heparinum sulphamidase for D-glucosamine sulphamate. Purification and characterisation. Eur. J. Biochem. 165, 633–638. · DOI
  157. Cheng Q. Hwa V. Salyers A.A. (1992) A locus that contributes to colonization of the intestinal tract by Bacteroides thetaiotaomicron contains a single regulatory gene (chuR) that links two polysaccharide utilization pathways. J. Bacteriol. 174, 7185–7193. · DOI
  158. Salyers A.A. O’Brien M. (1980) Cellular location of enzymes involved in chondroitin sulfate breakdown by Bacteroides thetaiotaomicron . J. Bacteriol. 143, 772–780. · DOI
  159. 10.1016/S0300-9084(73)80449-3 · DOI
  160. 10.1007/BF00499966 · DOI
  161. 10.1099/13500872-142-8-1989 · DOI
  162. 10.1046/j.1365-2958.1999.01398.x · DOI
  163. 10.1007/BF02328077 · DOI
  164. 10.1007/BF00394550 · DOI
  165. 10.1099/13500872-140-11-2991 · DOI
  166. 10.1007/s002030050730 · DOI
  167. 10.1042/bj3000429 · DOI
  168. 10.1007/s002030050415 · DOI
  169. 10.1099/13500872-142-2-251 · DOI
  170. Higgins T.P. Demarco P. Murrell J.C. (1997) Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenase. J. Bacteriol. 179, 1974–1979. · DOI
  171. 10.1099/00221287-140-6-1419 · DOI
  172. Anthony, C. (1982) The Biochemistry of Methylotrophs. Academic Press, London.
  173. De Marco P. Moradas Ferreira P. Higgins T.P. McDonald I. Kenna E.M. Murrell J.C. (1999) Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora . J. Bacteriol. 181, 2244–2251. · DOI
  174. 10.1016/0378-1119(94)00844-I · DOI
  175. Yen K.M. Karl M.R. Blatt L.M. Simon M.J. Winter R.B. Fausset P.R. Lu H.S. Harcourt A.A. Chen K.K. (1991) Cloning and characterization of a Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. J. Bacteriol. 173, 5315–5327. · DOI
  176. Shimamoto G. Berk R.S. (1979) Catabolism of taurine in Pseudomonas aeruginosa . Biochim. Biophys. Acta 569, 287–292. · DOI
  177. Shimamoto G. Berk R.S. (1980) Taurine catabolism. II. Biochemical and genetic evidence for sulfoacetaldehyde sulfolyase involvement. Biochim. Biophys. Acta 632, 121–130. · DOI
  178. 10.1016/0076-6879(87)43089-9 · DOI
  179. 10.1099/00221287-143-7-2339 · DOI
  180. 10.1099/00221287-143-12-3907 · DOI
  181. 10.1099/00221287-143-6-1919 · DOI
  182. 10.1007/s002030050502 · DOI
  183. Harwood J.L. Nicholls R.G. (1979) The plant sulpholipid, a major component of the sulphur cycle. Trans. Biochem. Soc. Lond. 7, 440–447. · DOI
  184. 10.1007/BF00288591 · DOI
  185. 10.1099/00221287-139-2-203 · DOI
  186. 10.1007/BF00288955 · DOI
  187. 10.1111/j.1574-6968.1993.tb06553.x · DOI
  188. 10.1046/j.1472-765X.1997.00062.x · DOI
  189. Seitz, A.P. and Leadbetter, E.R. (1995) Microbial assimilation and dissimilation of sulfonate sulfur. In: Geochemical Transformations of Sedimentary Sulfur. American Chemical Society Symposium Series 612 (Vairavamurthy, M.A. and Schoonen, M.A.A., Eds.), pp. 365–376, American Chemical Society, Washington, DC. · DOI
  190. 10.1111/j.1574-6968.1996.tb08109.x · DOI
  191. 10.1111/j.1574-6968.1994.tb07199.x · DOI
  192. van der Ploeg J.R. Weiss M.A. Saller E. Nashimoto H. Saito N. Kertesz M.A. Leisinger T. (1996) Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178, 5438–5446. · DOI
  193. 10.1093/jxb/44.5.849 · DOI
  194. 10.1016/S0031-9422(00)89621-1 · DOI
  195. van der Ploeg J.R. Iwanicka-Nowicka R. Bykowski T. Hryniewicz M. Leisinger T. (1999) The Cbl-regulated ssuEADCB gene cluster is required for aliphatic sulfonate-sulfur utilization in Escherichia coli . J. Biol. Chem. 174, 29358–29365. · DOI
  196. 10.1099/00221287-144-9-2555 · DOI
  197. Witschel M. Nagel S. Egli T. (1997) Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol. 179, 6937–6943. · DOI
  198. Knobel H.R. Egli T. van der Meer J.R. (1996) Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600. J. Bacteriol. 178, 6123–6132. · DOI
  199. Thibaut D. Ratet N. Bisch D. Faucher D. Debussche L. Blanche F. (1995) Purification of the two-enzyme system catalyzing the oxidation of the D-proline residue of pristinamycin II-B during the last step of pristinamycin II-A biosynthesis. J. Bacteriol. 177, 5199–5205. · DOI
  200. 10.1099/00221287-143-9-2961 · DOI

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Metadata

Authors
Kertesz, M. A.
Venue
FEMS Microbiology Reviews
Publisher
Oxford University Press (OUP)
Published
2000-04
Volume
24
Issue
2
Pages
135-175
ISSN
1574-6976
DOI
10.1016/s0168-6445(99)00033-9
Cited by
69
References
2
Language
en

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