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Gene Review

ALG5  -  dolichyl-phosphate beta-glucosyltransferase

Saccharomyces cerevisiae S288c

Synonyms: Asparagine-linked glycosylation protein 5, DolP-glucosyltransferase, Dolichyl-phosphate beta-glucosyltransferase, P1437, YPL227C
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Disease relevance of ALG5

  • Overexpression of Alg5p in both yeast and Escherichia coli results in an increase of UDP-glucose:dolichyl-phosphate glucosyltransferase activity, whereas a deletion of the yeast gene leads to a loss of this activity and a concomitant underglycosylation of carboxypeptidase Y [1].

High impact information on ALG5

  • Compared to the previously characterized ost1-1 mutant in the oligosaccharyltransferase, and the alg5 mutant in the oligosaccharide assembly pathway, ost3 null mutant yeast appear to be selectively impaired in the glycosylation of several membrane glycoproteins [2].
  • The Alg5 protein also localizes to the membrane of the endoplasmic reticulum, but does not interact with the oligosaccharyltransferase [3].
  • Binding was either reduced or absent in the microsomal membranes from two yeast mutants (alg5 and dpg1) that are known to be defective in the synthesis of glucosylphosphodolichol [4].
  • Monoglucosylated protein-linked oligosaccharides were detected in alg6 or alg5 mutant cells, which transfer Man9GlcNAc2 to protein; glucosylation was dependent on the inhibition of glucosidase II or the disruption of the gene encoding this enzyme [5].
  • A weak interaction was observed between Alg5p and Rer1p [6].

Biological context of ALG5

  • DNA sequencing of ALG5 revealed an open-reading frame of 1002 bases encoding a transmembrane protein of molecular mass 38.3 kDa [1].

Other interactions of ALG5

  • The ALG5 protein has sequence similarity to the GDP-mannose:dolichyl-phosphate mannosyltransferase (Dpm1p) from S. cerevisiae [1].
  • As compared with alg5 and alg6, alg8 secreted a higher proportion of ExgII, which was paralleled by a significant drop in the proportion of ExgTuni and, to a lesser extent, of ExgII1/2 [7].


  1. Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae. Heesen, S., Lehle, L., Weissmann, A., Aebi, M. Eur. J. Biochem. (1994) [Pubmed]
  2. Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. Karaoglu, D., Kelleher, D.J., Gilmore, R. J. Cell Biol. (1995) [Pubmed]
  3. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Stagljar, I., Korostensky, C., Johnsson, N., te Heesen, S. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. Evidence that the synthesis of glucosylphosphodolichol in yeast involves a 35-kDa membrane protein. Palamarczyk, G., Drake, R., Haley, B., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  5. Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence. Castro, O., Chen, L.Y., Parodi, A.J., Abeijón, C. Mol. Biol. Cell (1999) [Pubmed]
  6. Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. Massaad, M.J., Herscovics, A. J. Cell. Sci. (2001) [Pubmed]
  7. Glycosylation of yeast exoglucanase sequons in alg mutants deficient in the glucosylation steps of the lipid-linked oligosaccharide. Presence of glucotriose unit in Dol-PP-GlcNAc2Man9Glc3 influences both glycosylation efficiency and selection of N-linked sites. Muñoz, M.D., Hernández, L.M., Basco, R., Andaluz, E., Larriba, G. Biochim. Biophys. Acta (1994) [Pubmed]
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