Overexpression of the gene encoding GTP:mannose-1-phosphate guanyltransferase, mpg1, increases cellular GDP-mannose levels and protein mannosylation in Trichoderma reesei

Applied and Environmental Microbiology

Volumn 69, Issue 8, 2003, Pages 4383-4389

  Zakrzewska, Anna ^a   Palamarczyk, Grazyna ^a   Krotkiewski, Hubert ^b   Zdebska, Ewa ^c   Saloheimo, Markku ^d   Penttilä, Merja ^d   Kruszewska, Joanna S ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^b POLISH ACADEMY OF SCIENCES   (Poland)

^c INSTITUTE OF HEMATOLOGY AND TRANSFUSION MEDICINE   (Poland)

^d VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GENES; MICROBIOLOGY;

GENE ENCODING;

ENVIRONMENTAL ENGINEERING;

DOLICHYL PHOSPHATE MANNOSE SYNTHASE; FUNGAL ENZYME; GUANOSINE DIPHOSPHATE MANNOSE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE MANNOSE 1 PHOSPHATE GUANYLTRANSFERASE; MANNOSE PHOSPHATE; UNCLASSIFIED DRUG;

GENE EXPRESSION;

ARTICLE; BACTERIUM TRANSFORMATION; CARBOHYDRATE SYNTHESIS; DPM1 GENE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME REGULATION; GENE OVEREXPRESSION; MPG1 GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN GLYCOSYLATION; PROTEIN SECRETION; REGULATORY MECHANISM; TRANSCRIPTION REGULATION; TRICHODERMA REESEI;

BACTERIAL PROTEINS; GLYCOSYLATION; GUANOSINE DIPHOSPHATE MANNOSE; MANNOSE; NUCLEOTIDYLTRANSFERASES; TRICHODERMA;

BACTERIA (MICROORGANISMS); HYPOCREA; HYPOCREA JECORINA; TRICHODERMA;

EID: 0042029630     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.8.4383-4389.2003     Document Type: Article

References (30)

1. Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinum thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
2. Colussi, P. A., C. H. Taron, J. C. Mach, and P. Orlean. 1997. Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 94:7873-7878.
3. Dubois, M., K. A. Gilles, J. K. Hamilton, P. A. Robers, and F. Smith. 1956. Colorimetric method for determination of sugar and related substrates. Anal. Biochem. 28:350-356.
4. Duk, M., M. Ugorski, and E. Lisowska. 1997. β-Elimination of O-glycans from glycoproteins transferred to Immobilon P membranes: method and some applications. Anal. Biochem. 253:98-102.
5. Durand, H., M. Clanet, and G. Tiraby. 1988. Genetic improvement of Trichoderma reesei for large scale cellulase production. Enzyme Microbiol. Technol. 10:341-345.
6. Fagerstam, L. G., L. G. Pettersson, and J. A. Engström. 1984. The primary structure of a β-1,4-glucan cellobiohydrolase from the fungus Trichoderma reesei QM9414. FEBS Lett. 167:309-315.
7. Harman, G. E., and C. P. Kubicek. 1998. Enzymes, biocontrol and commercial applications, p. 129-163. In E. G. Harman and C. P. Kubicek (ed.), Trichoderma and Glocladium, vol. 2. Taylor and Francis, Ltd., London, United Kingdom.
8. Harrison, M. J., A. S. Nouwens, D. R. Jardine, N. E. Zachara, A. A. Gooley, H. Nevalainen, and N. H. Packer. 1998. Modified glycosylation of cellobiohydrolase I from a high cellulase-producing mutant strain of Trichoderma reesei. Eur. J. Biochem. 256:119-127.
9. Haselbeck, A., and W. Tanner. 1983. O glycosylation in Saccharomyces cerevisiae is initiated at the endoplasmic reticulum. FEBS Lett. 158:335-338.
10. Hirano, T., T. Sato, K. Yaegashi, and H. Enei. 2000. Efficient transformation of the edible basidiomycete Lentinus edodes with a vector using a glyceraldehyde-3-phosphate dehydrogenase promoter to hygromycin B resistance. Mol. Gen. Genet. 263:1047-1052.
11. Janik, A., J. Kruszewska, U. Lenart, M. Sosnowska, and G. Palamarczyk. 1999. Overexpression of α-D-mannose-1-phosphate guanyltransferase encoding gene restores the viability of the Saccharomyces cerevisiae mutants affected in early steps of glycoconjugate formation, p. 35-42 In H. J. Gilbert. G. J. Davies, B. Henrissat, and B. Svensson (ed.), Recent advances in carbohydrate bioengineering. Royal Society of Chemistry, Cambridge, United Kingdom.
12. Klarskov, K., K. Piens, J. Ståhlberg, P. B. Hoi, J. van Beeumen, and M. Claeyssens. 1997. Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including glycosylation pattern of the core protein. Carbohydr. Res. 304:143-153.
13. Kruszewska, J., R. Messner, C. P. Kubicek, and G. Palamarczyk. 1989. O glycosylation of proteins by membrane fraction of Trichoderma reesei QM9414. J. Gen. Microbiol. 135:301-307.
14. Kruszewska, J., G. Palamarczyk, and C. P. Kubicek. 1990. Stimulation of exoprotein secretion by choline and Tween 80 in Trichoderma reesei QM9414 correlates with increased activity of dolichol phosphate mannose synthase. J. Gen. Microbiol. 136:1293-1298.
15. Kruszewska, J., C. P. Kubicek, and G. Palamarczyk. 1994. Modulation of mannosylphosphodolichol synthase and dolichol kinase activity in Trichoderma reesei related to protein secretion. Acta Biochim. Pol. 41:331-339.
16. Kruszewska, J. S., M. Saloheimo, M. Penttilä, and G. Palamarczyk. 1998. Isolation of a Trichoderma reesei cDNA encoding GDP-α-D-marinose-1-phosphate guanyltransferase involved in early steps of protein glycosylation. Curr. Genet. 33:445-450.
17. Kruszewska, J., A. H. Butterweck, W. Kurztkowski, A. Migdalski, C. P. Kubicek, and G. Palamarczyk. 1999. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure. Appl. Environ. Microbiol. 65:2382-2387.
18. Kruszewska, J. S., M. Saloheimo, A. Migdalski, P. Orlean, M. Penttilä, and G. Palamarczyk. 2000. Dolichol phosphate mannose synthase from the filamentous fungus Trichoderma reesei belongs to the human and Schizosaccharomyces pombe class of the enzyme. Glycobiology 10:983-991.
19. Kubicek, C. P., T. Panda, G. Schreferl-Kunar, R. Messner, and F. Gruber. 1987. O-linked-but not N-linked-glycosylation is necessary for secretion of endoglucanase I and II by Trichoderma reesei. Can. J. Microbiol. 33:698-703.
20. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
21. Mach, R. L., M. Schindler, and C. P. Kubicek. 1994. Transformation of Trichoderma reesei based on hygromycin B resistance using homologous expression signals. Curr. Genet. 25:567-570.
22. Maeda, Y., S. Tanaka, J. Hino, K. Kangawa, and T. Kinoshita. 2000. Human dolichol-phosphate-mannose synthase consists of three subunits: DPM1, DPM2, and DPM3. EMBO J. 11:2475-2482.
23. Maras, M., A. de Bruyn, J. Schraml, P. Hersemijn, M. Claeyssens, W. Fiers, and R. Contreras. 1997. Structural characterisation of N-linked oligosaccharides from cellobioliydrolase I secreted by filamentous fungus Trichoderma reesei RUTC 30. Eur. J. Biochem. 245:617-625.
24. Messner, R., and C. P. Kubicek. 1988. Intracellular precursors of endo-β-1,4-glucanases in Trichoderma reesei. FEMS Microbiol. Lett. 50:227-232.
25. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed., vol. 1, p. 7.37-7.52. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
26. Sharma, C. B., P. Babczinski, L. Lehle, and W. Tanner. 1974. The role of dolicholmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem. 46:35-41.
27. Strahl-Bolsinger, S., M. Gentzch, and W. Tanner. 1999. Protein O-mannosylation. Biochim. Biophys. Acta. 1426:297-307.
28. Williamson, G., N. J. Belshaw, and M. P. Williamson. 1992. O-glycosylation in Aspergillus glucoamylase: conformation and role in binding. Biochem. J. 282:423-428.
29. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
30. Zdebska, E., and J. Koscielak. 1999. A single-sample method for determination of carbohydrate and protein contents in glycoprotein bands separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal. Biochem. 275:171-179.