Involvement of dolicholmonophosphate in the formation of specific mannosyl-linkages in yeast glycoproteins

Babczinski, Peter; Tanner, Widmar

doi:10.1016/0006-291x(73)90808-5

Cited by 107 publications

(35 citation statements)

References 13 publications

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“…In mammalian cells, protein O-glycosylation is generally initiated within the Golgi by the transfer of GalNAc from UDP-GalNAc [18]. In yeast, mannose is attached to the glycoproteins in the endoplasmic reticulum using dolichyl phosphate-o-mannose as immediate sugar donor [2,19,20]. To date, no homolgy between yeast protein O-mannosyltransferases and protein O-glycosyltransferases of higher eukaryotes has been found.…”

Section: Discussionmentioning

confidence: 99%

Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer

1995

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Section: Discussionmentioning

confidence: 99%

Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer

1995

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“…After this time about 6 % of the total radioactivity added is found in the lipid fraction, where it is bound almost exclusively to dolichol monophosphates [lo]. The methanol-insoluble material (70 % of the total radioactivity added) has been shown to consist at least of three glycoproteins [7]. One of these might be the yeast cell wall mannan.…”

Section: Characterization Of the Methanol-insoluble Mannosylated Matementioning

confidence: 99%

“…When the material released by this treatment is separated from large molecules by dialysis, and chromatographed on paper, three peaks are obtained. They have been identified as mannose, mannobiose and mannotriose [7]. The relative amounts of these three saccharides are given in Table 1.…”

Section: Characterization Of the Methanol-insoluble Mannosylated Matementioning

confidence: 99%

See 1 more Smart Citation

The Role of Dolicholmonophosphate in Glycoprotein Biosynthesis in Saccharomyces cerevisiae

Sharma

Babczinski

Lehle

et al. 1974

European Journal of Biochemistry

160

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1. In a crude particulate fraction from yeast mannose is transferred from GDP-mannose to an endogenous "lipid" fraction, the monophosphates of dolichol-14 to dolichol-18. The same membrane fraction also catalyzes the mannosylation of glycoproteins. More than 80 of the total radioactivity in the glycoprotein fraction obtained from GDP-[14C]mannose is released by /?-elimination. The small-sized radioactive products of /?-elimination are mannose, mannobiose and mannotriose.2. Ageing of the particulate fraction leads to a drastic loss of mannosyl transfer activity from GDP-[14C]mannose to dolichol monophosphate. To the same extent the amount of [14C]mannose obtained after /?-elimination of the glycoproteins decreases. The amount of radioactive mannobiose and mannotriose is, however, much less affected.3. With decreasing GDP-mannose concentrations the amount of [14C]mannose obtained after /&elimination increases as compared to the amount of radioactive mannobiose and mannotriose. The Km-value for the incorporation of mannosyl groups directly linked to serine and/or threonine, therefore, is lower than the Km-value for the transfer of subsequent mannosyl residues.4. 6. The results are consistent with the assumption that dolichol monophosphate is involved in the mannosylation of a specific position in yeast glycoproteins, i.e. in the formation of mannosyl linkages to serine and/or threonine. The subsequent mannosylation proceeds directly from GDP-mannose in a reaction obligatorily requiring Mn2+.7. After /?-elimination of the methanol-insoluble material mannosylated in the presence of dolichol-monophosphate [14C]mannose the residual insoluble radioactivity is to a large extent transformed into dialyzable material by pronase. Mannose, therefore, is transferred from dolicholmonophosphate mannose also to glycoprotein positions not involving OH-groups of serine or threonine.Glycosylated lipids play a role in the biosynthesis of glycoproteins in animals [l -51, fungi [6,7] and plants [S]. The lipophilic component in all these cases is probably dolichol monophosphate [2,4,9,10].In Succhuvomyces cerevisiue the lipophilic mannosyl acceptor has been shown by mass spectroscopy to consist of the monophosphates of the whole family of dolichols with 14 to 18 isoprene units [lo]. From -~ his 60th birthday. mannosylated dolichol monophosphates the mannosyl group is transferred by yeast membranes to glycoproteins. Preliminary evidence has been presented [7] threonine, only the mannosyl residue directly linked to Dedicated to Professor Dr 0. Hoffmann-Ostenhof on Abbreviations. Dolichol-P, dolichol monophosphate; dolichol-P-Man, dolichol-monophosphate-mannose ; GDPthat within oligomannose chains linked to serine/ Man, guanosine-diphosphate-mannose.Eur. J. Biochem. 46 (1974)

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“…This type of protein modification, which had long been considered to pertain exclusively to fungal cells, represented a main research topic over many years in my Institute at the University of Regensburg. Our interest in this protein modification started with the finding that Dol-P-mannose is the mannosyl donor for the first mannose that becomes O-linked to proteins in yeast (Babczinski and Tanner;1973;Orlean, 1990). This differed completely from the many O-glycosylation reactions described in higher eukaryotes, where the sugars are transferred from sugar nucleotides.…”

Section: The Pastmentioning

confidence: 99%

In 75 semesters, from mannan and dolichol to Pir proteins and membrane compartmentation: personal recollections

Tanner¹

2007

Yeast

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Involvement of dolicholmonophosphate in the formation of specific mannosyl-linkages in yeast glycoproteins

Cited by 107 publications

References 13 publications

Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer

Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer

The Role of Dolicholmonophosphate in Glycoprotein Biosynthesis in Saccharomyces cerevisiae

In 75 semesters, from mannan and dolichol to Pir proteins and membrane compartmentation: personal recollections

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