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dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
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in vitro asssay with both enzyme isoforms (RT and TW), 20 mM Tris, pH 8.0, mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, sugar donor is tritium-labeled, alpha-dystroglycan isoform C contains mucin-type domain that is target of O-mannose modifications in mammals, high grade of O-mannosylation, A isoform without noticeable O-mannosylation, rabbit alpha-dystroglycan as positive control shows lower O-mannosylation
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dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
the AaPmtA protein is involved in the formation of the normal cell wall. AaPmtA protein is responsible for the transfer of mannose to glucoamylase I
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the un-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals
AN5660
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dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
additional information
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dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
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dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
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dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
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dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
central role for Pmt4-mediated protein O-mannosylation in growth, cell wall integrity, and virulence of Cryptococcus neoformans
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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catalyzes the initial step of O-mannosyl glycan biosynthesis
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
role of O-glycosylation in the control of folding of secretory proteins in the endoplasmic reticulum
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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acceptor substrate specificities of PMT1-4,6
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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protein O-mannosylation is crucial for cell wall integrity, septation and viability
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dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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i.e. small-agglutinin
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dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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activity is not affected by disruption mutations of PMT1-4
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dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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protein is located at the cell surface
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dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
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PMT1 and PMT2, not PMT3 and PMT4
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dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
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protein is located in the medium
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dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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PMT1
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dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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PMT1, PMT4, PMT6 and especially PMT2, not PMT3
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dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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protein is located in the cell wall and medium
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dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
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PMT4 and PMT6, not PMT1-3
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dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
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protein is located at the cell surface
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dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
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PMT4, not PMT1-3
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dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
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protein is located in the Golgi apparatus
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dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
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mainly PMT1 and PMT2, not PMT3 and PMT4
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dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
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protein is located in the Golgi apparatus
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dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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PMT1
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dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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PMT1, PMT2, and to some extent PMT4, not PMT3
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dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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protein is located in the medium
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dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
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C-mannosylation activity
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dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
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biosynthetic pathway
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additional information
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Afpmt1 acts as an O-mannosyltransferase. Characterization of the DELTAAfpmt1 mutant shows that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 is not required for the virulence of Aspergillus fumigatus
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additional information
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PMT2 is essential for growth
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additional information
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PMT4 is required for full virulence of Candida albicans
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additional information
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PMT5 does not make a significant contribution to virulence
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additional information
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protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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additional information
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protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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additional information
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protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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additional information
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protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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additional information
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protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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additional information
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protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
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additional information
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although the improved secretion of the protein by suppression of O mannosylation might not be a general phenomenon, the suppression of O mannosylation could be beneficial for the production of proteins forming either homomeric or heteromeric complexes through their hydrophobic interaction in yeast
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additional information
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defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
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additional information
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disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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additional information
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disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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