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Gene Review

ALG1  -  chitobiosyldiphosphodolichol beta-1,4...

Saccharomyces cerevisiae S288c

Synonyms: Asparagine-linked glycosylation protein 1, Beta-1,4-mannosyltransferase, Chitobiosyldiphosphodolichol beta-mannosyltransferase, GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-dolichol diphosphochitobiose mannosyltransferase, ...
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Disease relevance of ALG1

  • The ALG1 gene product has been shown to catalyze the transfer of a mannosyl residue from GDP-mannose to the lipid-linked acceptor GlcNAc2, yielding Man beta 1-4GlcNAc2-lipid, in lysates from Escherichia coli transformants [1].

High impact information on ALG1


Biological context of ALG1

  • A plasmid suppressor of alg1, PSA1, encodes a 361 amino-acid protein with homology to NDP-hexose pyrophosphorylases, the enzymes that catalyze the formation of activated sugar nucleotides [6].
  • Thermosensitive mutants of Saccharomyces cerevisiae, affected in the endoplasmic reticulum (ER) located glycosylation, i.e. in Dol-P-Man synthase (dpm1), in beta-1,4 mannosyl transferase (alg1) and in alpha-1,3 mannosyltransferase (alg2), were used to assess the role of GDP-Man availability for the synthesis of dolichol-linked saccharides [7].
  • The DNA region including the ALG1 gene was sequenced and found to contain an open reading frame of 1347 bases [8].
  • Disruption of the 74-amino acid reading frame, which ended 42 bases upstream of the potential start codon for the ALG1 protein, showed it was not essential for viability [8].
  • The gene ALG1 has been cloned by complementation of the temperature-sensitive mutation alg1-1 with a total genomic DNA library [1].

Anatomical context of ALG1


Associations of ALG1 with chemical compounds


Physical interactions of ALG1

  • The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11 [14].

Other interactions of ALG1


Analytical, diagnostic and therapeutic context of ALG1


  1. Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway. Couto, J.R., Huffaker, T.C., Robbins, P.W. J. Biol. Chem. (1984) [Pubmed]
  2. Secretory vesicles externalize the major plasma membrane ATPase in yeast. Holcomb, C.L., Hansen, W.J., Etcheverry, T., Schekman, R. J. Cell Biol. (1988) [Pubmed]
  3. Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik. Schwarz, M., Thiel, C., Lübbehusen, J., Dorland, B., de Koning, T., von Figura, K., Lehle, L., Körner, C. Am. J. Hum. Genet. (2004) [Pubmed]
  4. A screen for yeast mutants with defects in the dolichol-mediated pathway for N-glycosylation. Roos, J., Sternglanz, R., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  5. Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik. Grubenmann, C.E., Frank, C.G., Hülsmeier, A.J., Schollen, E., Matthijs, G., Mayatepek, E., Berger, E.G., Aebi, M., Hennet, T. Hum. Mol. Genet. (2004) [Pubmed]
  6. Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1 N-glycosylation mutants. Benton, B.K., Plump, S.D., Roos, J., Lennarz, W.J., Cross, F.R. Curr. Genet. (1996) [Pubmed]
  7. 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., Palamarczyk, G. Biochim. Biophys. Acta (2003) [Pubmed]
  8. The sequence and transcript heterogeneity of the yeast gene ALG1, an essential mannosyltransferase involved in N-glycosylation. Albright, C.F., Robbins, R.W. J. Biol. Chem. (1990) [Pubmed]
  9. Dolichol is not a necessary moiety for lipid-linked oligosaccharide substrates of the mannosyltransferases involved in in vitro N-linked-oligosaccharide assembly. Wilson, I.B., Webberley, M.C., Revers, L., Flitsch, S.L. Biochem. J. (1995) [Pubmed]
  10. An evolving view of the eukaryotic oligosaccharyltransferase. Kelleher, D.J., Gilmore, R. Glycobiology (2006) [Pubmed]
  11. Functional evidence for UDP-galactose transporter in Saccharomyces cerevisiae through the in vivo galactosylation and in vitro transport assay. Roy, S.K., Yoko-o, T., Ikenaga, H., Jigami, Y. J. Biol. Chem. (1998) [Pubmed]
  12. Amplification and molecular cloning of the hamster tunicamycin-sensitive N-acetylglucosamine-1-phosphate transferase gene. The hamster and yeast enzymes share a common peptide sequence. Lehrman, M.A., Zhu, X.Y., Khounlo, S. J. Biol. Chem. (1988) [Pubmed]
  13. The chemoenzymatic synthesis of neoglycolipids and lipid-linked oligosaccharides using glycosyltransferases. Flitsch, S.L., Goodridge, D.M., Guilbert, B., Revers, L., Webberley, M.C., Wilson, I.B. Bioorg. Med. Chem. (1994) [Pubmed]
  14. Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum. Gao, X.D., Nishikawa, A., Dean, N. Glycobiology (2004) [Pubmed]
  15. Growth-related coordinate regulation of the early N-glycosylation genes in yeast. Kukuruzinska, M.A., Lennon, K. Glycobiology (1994) [Pubmed]
  16. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Deltaalg9 mutant reveals a regulatory role for the Alg3p alpha1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. Cipollo, J.F., Trimble, R.B. J. Biol. Chem. (2000) [Pubmed]
  17. Production of genetically modified lysozymes having extreme heat stability and antimicrobial activity against gram negative bacteria in yeast and in plant. Kato, A., Nakamura, S., Ibrahim, H., Matsumi, T., Tsumiyama, C., Kato, M. Die Nahrung. (1998) [Pubmed]
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