메뉴 건너뛰기




Volumn 1770, Issue 5, 2007, Pages 774-780

Protein glycosylation in pmt mutants of Saccharomyces cerevisiae. Influence of heterologously expressed cellobiohydrolase II of Trichoderma reesei and elevated levels of GDP-mannose and cis-prenyltransferase activity

Author keywords

cis prenyltransferase activity; GDP mannose level; O mannosylation; pmt mutants

Indexed keywords

CELLULOSE 1,4 BETA CELLOBIOSIDASE; DIMETHYLALLYLTRANSFERASE; DOLICHOL PHOSPHATE MANNOSE; FUNGAL PROTEIN; GENE PRODUCT; GUANOSINE DIPHOSPHATE MANNOSE; MANNOSYLTRANSFERASE; SYNTHETASE;

EID: 33947132734     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.01.010     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 0000510573 scopus 로고    scopus 로고
    • Protein secretion and glycosylation in Trichoderma
    • Kubicek C.P., and Harman G.E. (Eds), Taylor and Francis Ltd, London, UK
    • Palamarczyk G., Maras M., Contreras R., and Kruszewska J. Protein secretion and glycosylation in Trichoderma. In: Kubicek C.P., and Harman G.E. (Eds). Trichoderma and Glocladium vol. 1 (1998), Taylor and Francis Ltd, London, UK 121-138
    • (1998) Trichoderma and Glocladium , vol.1 , pp. 121-138
    • Palamarczyk, G.1    Maras, M.2    Contreras, R.3    Kruszewska, J.4
  • 2
    • 0000358186 scopus 로고
    • O-linked-but not N-linked-glycosylation is necessary for secretion of endoglucanase I and II by Trichoderma reesei
    • Kubicek C.P., Panda T., Schreferl-Kunar G., Messner R., and Gruber F. O-linked-but not N-linked-glycosylation is necessary for secretion of endoglucanase I and II by Trichoderma reesei. Can. J. Microbiol. 33 (1987) 698-703
    • (1987) Can. J. Microbiol. , vol.33 , pp. 698-703
    • Kubicek, C.P.1    Panda, T.2    Schreferl-Kunar, G.3    Messner, R.4    Gruber, F.5
  • 3
    • 0033020387 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell untrastructure
    • Kruszewska J.S., Butterweck A.H., Kurza{ogonek}tkowski W., Migdalski A., Kubicek C.P., and Palamarczyk G. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell untrastructure. Appl. Environ. Microbiol. 65 (1999) 2382-2387
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2382-2387
    • Kruszewska, J.S.1    Butterweck, A.H.2    Kurzatkowski, W.3    Migdalski, A.4    Kubicek, C.P.5    Palamarczyk, G.6
  • 4
    • 0035970569 scopus 로고    scopus 로고
    • Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
    • Agaphonov M.O., Packeiser A.N., Chechenova M.B., Choi E., and Ter-Avanesyan M.D. Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha. Yeast 18 (2001) 391-402
    • (2001) Yeast , vol.18 , pp. 391-402
    • Agaphonov, M.O.1    Packeiser, A.N.2    Chechenova, M.B.3    Choi, E.4    Ter-Avanesyan, M.D.5
  • 5
    • 27744494092 scopus 로고    scopus 로고
    • Mutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha
    • Agaphonov M.O., Sokolov S., Romanova N.V., Sohn J., Kim S.Y., Kalebina T.S., Choi E.S., and Ter-Avanesyan M.D. Mutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha. Yeast 22 (2005) 1037-1047
    • (2005) Yeast , vol.22 , pp. 1037-1047
    • Agaphonov, M.O.1    Sokolov, S.2    Romanova, N.V.3    Sohn, J.4    Kim, S.Y.5    Kalebina, T.S.6    Choi, E.S.7    Ter-Avanesyan, M.D.8
  • 6
    • 0033553672 scopus 로고    scopus 로고
    • O-glycosylation of Axl1/Bud10p by Pmt4p is required for its stability, localisation and function in daughter cells
    • Sanders S., Gentzsch M., Tanner W., and Herskowitz I. O-glycosylation of Axl1/Bud10p by Pmt4p is required for its stability, localisation and function in daughter cells. J. Cell Biol. 145 (1999) 1177-1188
    • (1999) J. Cell Biol. , vol.145 , pp. 1177-1188
    • Sanders, S.1    Gentzsch, M.2    Tanner, W.3    Herskowitz, I.4
  • 7
    • 1642505521 scopus 로고    scopus 로고
    • O-Glycosylation as a sorting determinant for cell surface delivery in yeast
    • Proszynski T.J., Simons K., and Bagnat M. O-Glycosylation as a sorting determinant for cell surface delivery in yeast. Mol. Biol. Cell 15 (2004) 1533-1543
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1533-1543
    • Proszynski, T.J.1    Simons, K.2    Bagnat, M.3
  • 8
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch M., and Tanner W. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 15 (1996) 5752-5759
    • (1996) EMBO J. , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 9
    • 0030925063 scopus 로고    scopus 로고
    • Protein-O-glycosylation in yeast: protein-specific mannosyltransferases
    • Gentzsch M., and Tanner W. Protein-O-glycosylation in yeast: protein-specific mannosyltransferases. Glycobiology 7 (1997) 481-486
    • (1997) Glycobiology , vol.7 , pp. 481-486
    • Gentzsch, M.1    Tanner, W.2
  • 10
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Guide to Yeast Genetics and Molecular Biology. Gutherie C., and Fink G.R. (Eds)
    • Sherman F. Getting started with yeast. In: Gutherie C., and Fink G.R. (Eds). Guide to Yeast Genetics and Molecular Biology. Methods Enzymol. vol. 194 (1991) 3-21
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 11
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen D., Yang B., and Kuo T. One-step transformation of yeast in stationary phase. Curr. Genet. 21 (1992) 83-84
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.1    Yang, B.2    Kuo, T.3
  • 13
    • 0023875673 scopus 로고
    • Efficient secretion of two fungal cellobiohydrolases by Saccharomyces cerevisiae
    • Penttila M.E., Andre L., Lehtovaara P., Bailey M., Teeri T.T., and Knowles J.K.C. Efficient secretion of two fungal cellobiohydrolases by Saccharomyces cerevisiae. Gene 63 (1988) 103-112
    • (1988) Gene , vol.63 , pp. 103-112
    • Penttila, M.E.1    Andre, L.2    Lehtovaara, P.3    Bailey, M.4    Teeri, T.T.5    Knowles, J.K.C.6
  • 14
    • 0037591637 scopus 로고    scopus 로고
    • cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2
    • Zakrzewska A., Migdalski A., Saloheimo M., Penttila M.E., Palamarczyk G., and Kruszewska J.S. cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2. Curr. Genet. 43 (2003) 11-16
    • (2003) Curr. Genet. , vol.43 , pp. 11-16
    • Zakrzewska, A.1    Migdalski, A.2    Saloheimo, M.3    Penttila, M.E.4    Palamarczyk, G.5    Kruszewska, J.S.6
  • 15
    • 0037424802 scopus 로고    scopus 로고
    • Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation
    • Janik A., Sosnowska M., Kruszewska J., Krotkiewski H., Lehle L., and Plamarczyk G. Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation. Biochim. Biophys. Acta 1621 (2003) 22-30
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 22-30
    • Janik, A.1    Sosnowska, M.2    Kruszewska, J.3    Krotkiewski, H.4    Lehle, L.5    Plamarczyk, G.6
  • 16
    • 85025744796 scopus 로고
    • Specificity in the interaction of direct dyes with polysaccharides
    • Wood P.J. Specificity in the interaction of direct dyes with polysaccharides. Carbohydr. Res. 85 (1980) 271-287
    • (1980) Carbohydr. Res. , vol.85 , pp. 271-287
    • Wood, P.J.1
  • 17
    • 0024603109 scopus 로고
    • O-glycosylation of proteins by membrane fraction of Trichoderma reesei QM9414
    • Kruszewska J., Messner R., Kubicek C.P., and Palamarczyk G. O-glycosylation of proteins by membrane fraction of Trichoderma reesei QM9414. J. Gen. Microbiol. 135 (1989) 301-307
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 301-307
    • Kruszewska, J.1    Messner, R.2    Kubicek, C.P.3    Palamarczyk, G.4
  • 18
    • 0016248170 scopus 로고
    • The role of dolicholmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae
    • Sharma C.B., Babczinski P., Lehle L., and Tanner W. The role of dolicholmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem. 46 (1974) 35-41
    • (1974) Eur. J. Biochem. , vol.46 , pp. 35-41
    • Sharma, C.B.1    Babczinski, P.2    Lehle, L.3    Tanner, W.4
  • 19
    • 0042029630 scopus 로고    scopus 로고
    • Overexpression of the gene encoding GTP:mannose-1-phosphate guanyltransferase, mpg1, increases cellular GDP-mannose levels and protein mannosylation in Trichoderma reesei
    • Zakrzewska A., Palamarczyk G., Kotkiewski H., Zdebska E., Saloheimo M., Penttila M., and Kruszewska J.S. Overexpression of the gene encoding GTP:mannose-1-phosphate guanyltransferase, mpg1, increases cellular GDP-mannose levels and protein mannosylation in Trichoderma reesei. Appl. Environ. Microbiol. 69 (2003) 4383-4389
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4383-4389
    • Zakrzewska, A.1    Palamarczyk, G.2    Kotkiewski, H.3    Zdebska, E.4    Saloheimo, M.5    Penttila, M.6    Kruszewska, J.S.7
  • 20
    • 0030994977 scopus 로고    scopus 로고
    • Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression
    • Szkopińska A., Grabińska K., Delourme D., Karst F., Rytka J., and Palamarczyk G. Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression. J. Lipid Res. 38 (1997) 962-968
    • (1997) J. Lipid Res. , vol.38 , pp. 962-968
    • Szkopińska, A.1    Grabińska, K.2    Delourme, D.3    Karst, F.4    Rytka, J.5    Palamarczyk, G.6
  • 21
    • 0025777266 scopus 로고
    • Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I
    • Aho S., Olkkonen V., Jalava T., Paloheimo M., Buhler R., Niku-Paavola M., Bamford D.H., and Korhola M. Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I. Eur. J. Biochem. 200 (1991) 643-649
    • (1991) Eur. J. Biochem. , vol.200 , pp. 643-649
    • Aho, S.1    Olkkonen, V.2    Jalava, T.3    Paloheimo, M.4    Buhler, R.5    Niku-Paavola, M.6    Bamford, D.H.7    Korhola, M.8
  • 23
    • 0031281536 scopus 로고    scopus 로고
    • β-elimination of O-glycans from glycoproteins transferred to Immobilon P membranes: method and some applications
    • Duk M., Ugorski M., and Lisowska E. β-elimination of O-glycans from glycoproteins transferred to Immobilon P membranes: method and some applications. Anal. Biochem. 253 (1997) 98-102
    • (1997) Anal. Biochem. , vol.253 , pp. 98-102
    • Duk, M.1    Ugorski, M.2    Lisowska, E.3
  • 24
    • 0345148486 scopus 로고    scopus 로고
    • A single-sample method for determination of carbohydrate and protein contents in glycoprotein bands separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Zdebska E., and Kościelak J. 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 (1999) 171-179
    • (1999) Anal. Biochem. , vol.275 , pp. 171-179
    • Zdebska, E.1    Kościelak, J.2
  • 25
    • 0023139828 scopus 로고
    • Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei
    • Chen C.M., Gritzali M., and Stafford D.W. Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei. Biotechnology 5 (1987) 274-278
    • (1987) Biotechnology , vol.5 , pp. 274-278
    • Chen, C.M.1    Gritzali, M.2    Stafford, D.W.3
  • 26
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II
    • Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., and Knowles J. Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51 (1987) 43-52
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovuori, I.4    Knowles, J.5
  • 27
    • 0000372094 scopus 로고
    • The primary structure of a β-1,4-glucan cellobiohydrolase from the fungus Trichoderma reesei QM9414
    • Fagerstam L.G., Pettersson L.G., and Engström J.A. The primary structure of a β-1,4-glucan cellobiohydrolase from the fungus Trichoderma reesei QM9414. FEBS Lett. 167 (1984) 309-315
    • (1984) FEBS Lett. , vol.167 , pp. 309-315
    • Fagerstam, L.G.1    Pettersson, L.G.2    Engström, J.A.3
  • 28
    • 0038823596 scopus 로고    scopus 로고
    • Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes
    • Girrbach V., and Strahl S. Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes. J. Biol. Chem. 278 (2003) 12554-12562
    • (2003) J. Biol. Chem. , vol.278 , pp. 12554-12562
    • Girrbach, V.1    Strahl, S.2
  • 29
    • 0019320806 scopus 로고
    • Stimulation by GDP-mannose of the biosynthesis of N-acetylglucosaminylpyrophosphoryl polyprenols by the retina
    • Kean E.L. Stimulation by GDP-mannose of the biosynthesis of N-acetylglucosaminylpyrophosphoryl polyprenols by the retina. J. Biol. Chem. 255 (1980) 1921-1927
    • (1980) J. Biol. Chem. , vol.255 , pp. 1921-1927
    • Kean, E.L.1
  • 30
    • 0019787655 scopus 로고
    • Transfer of glucose in the biosynthesis of thyroid glycoproteins: I. Inhibition of glucose transfer to oligosaccharide lipids by GDP-mannose
    • Ronin C., Caseti C., and Bouchilloux S. Transfer of glucose in the biosynthesis of thyroid glycoproteins: I. Inhibition of glucose transfer to oligosaccharide lipids by GDP-mannose. Biochim. Biophys. Acta 674 (1981) 47-48
    • (1981) Biochim. Biophys. Acta , vol.674 , pp. 47-48
    • Ronin, C.1    Caseti, C.2    Bouchilloux, S.3
  • 31
    • 33646372952 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation
    • Perlińska-Lenart U., Bańkowska R., Palamarczyk G., and Kruszewska J.S. Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation. Fungal Genet. Biol. 43 (2006) 422-429
    • (2006) Fungal Genet. Biol. , vol.43 , pp. 422-429
    • Perlińska-Lenart, U.1    Bańkowska, R.2    Palamarczyk, G.3    Kruszewska, J.S.4
  • 32
    • 0035094506 scopus 로고    scopus 로고
    • An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols
    • Shenk B., Rush J.S., Waechter Ch.J., and Aeby M. An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols. Glycobiology 11 (2001) 89-98
    • (2001) Glycobiology , vol.11 , pp. 89-98
    • Shenk, B.1    Rush, J.S.2    Waechter, Ch.J.3    Aeby, M.4
  • 33
    • 0023512608 scopus 로고
    • Characterization of the Saccharomyces cerevisiae cis-prenyltransferase required for dolichyl phosphate biosynthesis
    • Adair W.L.J., and Cafmeyer N. Characterization of the Saccharomyces cerevisiae cis-prenyltransferase required for dolichyl phosphate biosynthesis. Arch. Biochem. Biophys. 259 (1987) 589-596
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 589-596
    • Adair, W.L.J.1    Cafmeyer, N.2
  • 34
    • 0017649682 scopus 로고
    • Biosynthesis of dolichol phosphate by subcellular fractions from liver
    • Daleo G.R., Hopp H.E., Romero P.A., and Lezica R. Biosynthesis of dolichol phosphate by subcellular fractions from liver. FEBS Lett. 81 (1977) 411-414
    • (1977) FEBS Lett. , vol.81 , pp. 411-414
    • Daleo, G.R.1    Hopp, H.E.2    Romero, P.A.3    Lezica, R.4
  • 36
    • 0343848122 scopus 로고    scopus 로고
    • Products of S. cerevisiae cis-prenyltransferase activity in vitro
    • Szkopińska A., Karst F., and Palamarczyk G. Products of S. cerevisiae cis-prenyltransferase activity in vitro. Biochimie 78 (1996) 111-116
    • (1996) Biochimie , vol.78 , pp. 111-116
    • Szkopińska, A.1    Karst, F.2    Palamarczyk, G.3
  • 37
    • 0034945070 scopus 로고    scopus 로고
    • Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localization. Implication for their distinct physiological roles in dolichol synthesis
    • Sato M., Fujisaki S., Sato K., Nishimura Y., and Nakano A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localization. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495-506
    • (2001) Genes Cells , vol.6 , pp. 495-506
    • Sato, M.1    Fujisaki, S.2    Sato, K.3    Nishimura, Y.4    Nakano, A.5
  • 39
    • 0344063650 scopus 로고    scopus 로고
    • Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltransferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells
    • Shridas P., Rush J.S., and Waechter Ch.J. Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltransferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem. Biophys. Res. Commun. 312 (2003) 1349-1356
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1349-1356
    • Shridas, P.1    Rush, J.S.2    Waechter, Ch.J.3
  • 40
    • 2442664229 scopus 로고    scopus 로고
    • Screening for novel essential genes of Saccharomyces cerevisiae involved in protein secretion
    • Davydenko S.G., Juselius J.K., Munder T., Bogengruber E., Jantti J., and Keranen S. Screening for novel essential genes of Saccharomyces cerevisiae involved in protein secretion. Yeast 21 (2004) 463-471
    • (2004) Yeast , vol.21 , pp. 463-471
    • Davydenko, S.G.1    Juselius, J.K.2    Munder, T.3    Bogengruber, E.4    Jantti, J.5    Keranen, S.6
  • 41
    • 0032909653 scopus 로고    scopus 로고
    • The yeast RER2 gene, identified by endoplasmic reticulum protein localisation mutations, encodes cis-prenyltansferase, a key enzyme in dolichol synthesis
    • Sato M., Sato K., Nishikawa S., Kato J., and Nakano A. The yeast RER2 gene, identified by endoplasmic reticulum protein localisation mutations, encodes cis-prenyltansferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471-483
    • (1999) Mol. Cell Biol. , vol.19 , pp. 471-483
    • Sato, M.1    Sato, K.2    Nishikawa, S.3    Kato, J.4    Nakano, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.