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. 1986 Nov;168(2):734–738. doi: 10.1128/jb.168.2.734-738.1986

Transport and hydrolysis of disaccharides by Trichosporon cutaneum.

M Mörtberg, H Y Neujahr
PMCID: PMC213543  PMID: 3782022

Abstract

Trichosporon cutaneum is shown to utilize six disaccharides, cellobiose, maltose, lactose, sucrose, melibiose, and trehalose. T. cutaneum can thus be counted with the rather restricted group of yeasts (11 to 12% of all investigated) which can utilize lactose and melibiose. The half-saturation constants for uptake were 10 +/- 3 mM sucrose or lactose and 5 +/- 1 mM maltose, which is of the same order of magnitude as those reported for Saccharomyces cerevisiae. Our results indicate that maltose shares a common transport system with sucrose and that there may be some interaction between the uptake systems for lactose, cellobiose, and glucose. Lactose, cellobiose, and melibiose are hydrolyzed by cell wall-bound glycosidase(s), suggesting hydrolysis before or in connection with uptake. In contrast, maltose, sucrose, and trehalose seem to be taken up as such. The uptake of sucrose and lactose is dependent on a proton gradient across the cell membrane. In contrast, there were no indications of the involvement of gradients of H+, K+, or Na+ in the uptake of maltose. The uptake of lactose is to a large extent inducible, as is the corresponding glycosidase. Also the glycosidases for cellobiose, trehalose, and melibiose are inducible. In contrast, the uptake of sucrose and maltose and the corresponding glycosidases is constitutive.

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Selected References

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  1. Anderson J. J., Dagley S. Catabolism of aromatic acids in Trichosporon cutaneum. J Bacteriol. 1980 Feb;141(2):534–543. doi: 10.1128/jb.141.2.534-543.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  3. Cohen J. D., Goldenthal M. J., Buchferer B., Marmur J. Mutational analysis of the MAL1 locus of Saccharomyces: identification and functional characterization of three genes. Mol Gen Genet. 1984;196(2):208–216. doi: 10.1007/BF00328052. [DOI] [PubMed] [Google Scholar]
  4. DE LA FUENTE G., SOLS A. Transport of sugars in yeasts. II. Mechanisms of utilization of disaccharides and related glycosides. Biochim Biophys Acta. 1962 Jan 1;56:49–62. doi: 10.1016/0006-3002(62)90526-7. [DOI] [PubMed] [Google Scholar]
  5. Dickson R. C., Dickson L. R., Markin J. S. Purification and properties of an inducible beta-galactosidase isolated from the yeast Kluyveromyces lactis. J Bacteriol. 1979 Jan;137(1):51–61. doi: 10.1128/jb.137.1.51-61.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dickson R. C., Markin J. S. Molecular cloning and expression in E. coli of a yeast gene coding for beta-galactosidase. Cell. 1978 Sep;15(1):123–130. doi: 10.1016/0092-8674(78)90088-0. [DOI] [PubMed] [Google Scholar]
  7. Freer S. N., Detroy R. W. Regulation of beta-1, 4-Glucosidase Expression by Candida wickerhamii. Appl Environ Microbiol. 1985 Jul;50(1):152–159. doi: 10.1128/aem.50.1.152-159.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gaal A. B., Neujahr H. Y. Maleylacetate reductase from Trichosporon cutaneum. Biochem J. 1980 Mar 1;185(3):783–786. doi: 10.1042/bj1850783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gaal A., Neujahr H. Y. Induction of phenol-metabolizing enzymes in Trichosporon cutaneum. Arch Microbiol. 1981 Sep;130(1):54–58. doi: 10.1007/BF00527072. [DOI] [PubMed] [Google Scholar]
  10. Gaal A., Neujahr H. Y. Metabolism of phenol and resorcinol in Trichosporon cutaneum. J Bacteriol. 1979 Jan;137(1):13–21. doi: 10.1128/jb.137.1.13-21.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gaal A., Neujahr H. Y. cis,cis-Muconate cyclase from Trichosporon cutaneum. Biochem J. 1980 Oct 1;191(1):37–43. doi: 10.1042/bj1910037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Janda S., von Hedenström M. Uptake of disaccharides by the aerobic yeast Rhodotorula glutinis. Hydrolysis of beta-fructosides and trehalose. Arch Microbiol. 1974;101(3):273–280. doi: 10.1007/BF00455944. [DOI] [PubMed] [Google Scholar]
  13. Johnson H. S., Hatch M. D. Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochem J. 1970 Sep;119(2):273–280. doi: 10.1042/bj1190273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kotyk A., Michaljanicová D. Uptake of trehalose by Saccharomyces cerevisiae. J Gen Microbiol. 1979 Feb;110(2):323–332. doi: 10.1099/00221287-110-2-323. [DOI] [PubMed] [Google Scholar]
  15. Miozzari G. F., Niederberger P., Hütter R. Permeabilization of microorganisms by Triton X-100. Anal Biochem. 1978 Oct 1;90(1):220–233. doi: 10.1016/0003-2697(78)90026-x. [DOI] [PubMed] [Google Scholar]
  16. Mörtberg M., Neujahr H. Y. Uptake of phenol by Trichosporon cutaneum. J Bacteriol. 1985 Feb;161(2):615–619. doi: 10.1128/jb.161.2.615-619.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Neujahr H. Y., Gaal A. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur J Biochem. 1973 Jun;35(2):386–400. doi: 10.1111/j.1432-1033.1973.tb02851.x. [DOI] [PubMed] [Google Scholar]
  18. Neujahr H. Y., Varga J. M. Degradation of phenols by intact cells and cell-free preparations of Trichosporon cutaneum. Eur J Biochem. 1970 Mar 1;13(1):37–44. doi: 10.1111/j.1432-1033.1970.tb00896.x. [DOI] [PubMed] [Google Scholar]
  19. Powlowski J. B., Dagley S. beta-Ketoadipate pathway in Trichosporon cutaneum modified for methyl-substituted metabolites. J Bacteriol. 1985 Sep;163(3):1126–1135. doi: 10.1128/jb.163.3.1126-1135.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Powlowski J. B., Ingebrand J., Dagley S. Enzymology of the beta-ketoadipate pathway in Trichosporon cutaneum. J Bacteriol. 1985 Sep;163(3):1136–1141. doi: 10.1128/jb.163.3.1136-1141.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Santos E., Rodriguez L., Elorza M. V., Sentandreu R. Uptake of sucrose by Saccharomyces cerevisiae. Arch Biochem Biophys. 1982 Jul;216(2):652–660. doi: 10.1016/0003-9861(82)90255-7. [DOI] [PubMed] [Google Scholar]
  22. Serrano R. Energy requirements for maltose transport in yeast. Eur J Biochem. 1977 Oct 17;80(1):97–102. doi: 10.1111/j.1432-1033.1977.tb11861.x. [DOI] [PubMed] [Google Scholar]
  23. Sparnins V. L., Anderson J. J., Omans J., Dagley S. Degradation of 4-hydroxyphenylacetic acid by Trichosporon cutaneum. J Bacteriol. 1978 Oct;136(1):449–451. doi: 10.1128/jb.136.1.449-451.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sparnins V. L., Burbee D. G., Dagley S. Catabolism of L-tyrosine in Trichosporon cutaneum. J Bacteriol. 1979 May;138(2):425–430. doi: 10.1128/jb.138.2.425-430.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stephen E. R., Nasim A. Production of protoplasts in different yeasts by mutanase. Can J Microbiol. 1981 May;27(5):550–553. doi: 10.1139/m81-082. [DOI] [PubMed] [Google Scholar]
  26. Varga J. M., Neujahr H. Y. Purification and properties of catechol 1,2-oxygenase from Trichosporon cutaneum. Eur J Biochem. 1970 Feb;12(3):427–434. doi: 10.1111/j.1432-1033.1970.tb00869.x. [DOI] [PubMed] [Google Scholar]

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