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Gene Review

DPM1  -  dolichyl-phosphate beta-D-mannosyltransferase

Saccharomyces cerevisiae S288c

Synonyms: DPM synthase, Dolichol-phosphate mannose synthase, Dolichol-phosphate mannosyltransferase, Dolichyl-phosphate beta-D-mannosyltransferase, MPD synthase, ...
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Disease relevance of DPM1

  • DPM1 is the structural gene for yeast Dol-P-Man synthase since Escherichia coli transformants harboring this gene express Dol-P-Man synthase activity in vitro [1].
  • This intermediate was previously shown to accumulate, however, in murine lymphoma mutant E and in yeast mutant dpm1, both of which lack dolicholphosphomannose synthase activity [2].

High impact information on DPM1

  • Here, we show that a COOH-terminal region in yeast Sac1p is crucial for ER targeting by directly interacting with dolicholphosphate mannose synthase Dpm1p [3].
  • DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate [4].
  • DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1 [4].
  • (ii) The ALG7 and DPM1 proteins are known to recognize the isoprenoid region of dolichol phosphate specifically; this recognition presumably occurs in the membrane since dolichol is very hydrophobic [5].
  • We present evidence that the S. cerevisiae gene DPM1, when stably transfected into a mutant Chinese hamster ovary cell line, B4-2-1, is able to correct the glycosylation defect of the cells [6].

Biological context of DPM1

  • Pathway activation was also suppressed in dpm1-101 mutants by plasmids that contained RER2 or PSA1, which produce the substrates for Dpm1 [7].
  • The possibility that cloned cDNA encodes a product with a MPD synthase activity was also excluded by transforming a heterozygous S. cerevisiae dpm1::LEU2/DPM1 diploid, which did not lead to the restoration of viability of the dpm1 spores [8].
  • Temperature-sensitive yeast mutants were isolated after in vitro mutagenesis of the yeast DPM1 gene [9].
  • Instead, DPM1 may be an essential gene because its product is required for O-glycosylation in yeast or because Dol-P-Man synthase is needed in some unidentified pathway [1].
  • DNA sequencing of the DPM1 gene revealed an open reading frame of 801 bases [1].

Anatomical context of DPM1


Associations of DPM1 with chemical compounds


Other interactions of DPM1

  • The ALG5 protein has sequence similarity to the GDP-mannose:dolichyl-phosphate mannosyltransferase (Dpm1p) from S. cerevisiae [15].
  • The interaction with Dpm1p persists during exponential cell division but is rapidly abolished when cell growth slows because of nutrient limitation, causing translocation of Sac1p to Golgi membranes [3].
  • The secretion mutant sec59 has a similar phenotype to dpm1, and the presence of a dolichol recognition sequence in the SEC59 protein gave a clue to its defect, which is in dolichol kinase [16].

Analytical, diagnostic and therapeutic context of DPM1

  • Expression of dolichol phosphate mannose synthase of S. mansoni (SmDPMS) was analysed by Northern blot and quantified by semi-quantitative RT-PCR with cDNA from mature and immature male and female worms [17].
  • SDS/ PAGE of the purified enzyme fraction revealed the presence of a protein band of 31 kDa corresponding to the apparent molecular mass of the MPD-synthase purified from S. cerevisiae [Babczinski, P. et al. (1980) Eur. J. Biochem. 105, 509-515; Haselbeck A. (1989) Eur. J. Biochem. 181, 663-668] [18].


  1. Cloning and sequencing of the yeast gene for dolichol phosphate mannose synthase, an essential protein. Orlean, P., Albright, C., Robbins, P.W. J. Biol. Chem. (1988) [Pubmed]
  2. Accumulation of glucosaminyl(acyl)phosphatidylinositol in an S3 HeLa subline expressing normal dolicholphosphomannose synthase activity. Sevlever, D., Schiemann, D., Guidubaldi, J., Medof, M.E., Rosenberry, T.L. Biochem. J. (1997) [Pubmed]
  3. Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p. Faulhammer, F., Konrad, G., Brankatschk, B., Tahirovic, S., Knödler, A., Mayinger, P. J. Cell Biol. (2005) [Pubmed]
  4. DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate. Maeda, Y., Tomita, S., Watanabe, R., Ohishi, K., Kinoshita, T. EMBO J. (1998) [Pubmed]
  5. A 13-amino acid peptide in three yeast glycosyltransferases may be involved in dolichol recognition. Albright, C.F., Orlean, P., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  6. The Saccharomyces cerevisiae DPM1 gene encoding dolichol-phosphate-mannose synthase is able to complement a glycosylation-defective mammalian cell line. Beck, P.J., Orlean, P., Albright, C., Robbins, P.W., Gething, M.J., Sambrook, J.F. Mol. Cell. Biol. (1990) [Pubmed]
  7. Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast. Cullen, P.J., Schultz, J., Horecka, J., Stevenson, B.J., Jigami, Y., Sprague, G.F. Genetics (2000) [Pubmed]
  8. Isolation of a Trichoderma reesei cDNA encoding GTP: a-D-mannose-1-phosphate guanyltransferase involved in early steps of protein glycosylation. Kruszewska, J.S., Saloheimo, M., Penttilä, M., Palamarczyk, G. Curr. Genet. (1998) [Pubmed]
  9. Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae. Orlean, P. Mol. Cell. Biol. (1990) [Pubmed]
  10. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure. Kruszewska, J.S., Butterweck, A.H., Kurzatkowski, W., Migdalski, A., Kubicek, C.P., Palamarczyk, G. Appl. Environ. Microbiol. (1999) [Pubmed]
  11. Glycoprotein Hypersecretion Alters the Cell Wall in Trichoderma reesei Strains Expressing the Saccharomyces cerevisiae Dolichylphosphate Mannose Synthase Gene. Perlinska-Lenart, U., Orlowski, J., Laudy, A.E., Zdebska, E., Palamarczyk, G., Kruszewska, J.S. Appl. Environ. Microbiol. (2006) [Pubmed]
  12. Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation. Perlińska-Lenart, U., Kurzatkowski, W., Janas, P., Kopińska, A., Palamarczyk, G., Kruszewska, J.S. Acta Biochim. Pol. (2005) [Pubmed]
  13. The isolation of a Dol-P-Man synthase from Ustilago maydis that functions in Saccharomyces cerevisiae. Zimmerman, J.W., Specht, C.A., Cazares, B.X., Robbins, P.W. Yeast (1996) [Pubmed]
  14. Translocation of the yeast dolichol-phosphate-mannose synthase into microsomal membranes. Déglon, N., Krapp, A., Bron, C., Fasel, N. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  15. 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]
  16. Enzymes that recognize dolichols participate in three glycosylation pathways and are required for protein secretion. Orlean, P. Biochem. Cell Biol. (1992) [Pubmed]
  17. Dolichol phosphate mannose synthase is differentially expressed in male and female worms of Schistosoma mansoni. Tempone, A.J., Furtado, D.R., Gimba, E.R., Oliveira, F.M., Rumjanek, F.D. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2002) [Pubmed]
  18. Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei. Kruszewska, J.S., Perlińska-Lenart, U., Palamarczyk, G. Acta Biochim. Pol. (1996) [Pubmed]
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