Poly-Saturated Dolichols from Filamentous Fungi Modulate Activity of Dolichol-Dependent Glycosyltransferase and Physical Properties of Membranes

  title={Poly-Saturated Dolichols from Filamentous Fungi Modulate Activity of Dolichol-Dependent Glycosyltransferase and Physical Properties of Membranes},
  author={Elżbieta Gryz and U. Perlińska-Lenart and Katarzyna Gawarecka and A. Jozwiak and Sebastian Piłsyk and A. Lipko and M. Jemioła-Rzemińska and P. Bernat and A. Muszewska and Kamil Steczkiewicz and K. Ginalski and J. Długoński and K. Strzal̵ka and E. Swiezewska and J. Kruszewska},
  journal={International Journal of Molecular Sciences},
Mono-saturated polyprenols (dolichols) have been found in almost all Eukaryotic cells, however, dolichols containing additional saturated bonds at the ω-end, have been identified in A. fumigatus and A. niger. Here we confirm using an LC-ESI-QTOF-MS analysis, that poly-saturated dolichols are abundant in other filamentous fungi, Trichoderma reesei, A. nidulans and Neurospora crassa, while the yeast Saccharomyces cerevisiae only contains the typical mono-saturated dolichols. We also show, using… Expand
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Metabolomics profiling reveals new aspects of dolichol biosynthesis in Plasmodium falciparum
The metabolomics studies revealed that cis-polyisoprenoids are more diverse in the malaria parasite Plasmodium falciparum than previously postulated as it was uncovered active de novo biosynthesis and substantial levels of accumulation of polyprenols and dolichols of 15 to 19 isoprene units. Expand
Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae
Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-N-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells, and results show that Yil 102c-C is a functional homolog of DPMII from T. reesei and Dpm2 from humans. Expand
Lipids, proteins and extracellular metabolites of Trichoderma harzianum modifications caused by 2,4-dichlorophenoxyacetic acid as a plant growth stimulator.
The synthesis of some proteins, such as calcineurin-like phosphoesterase metallophosphatases (MPPs), which modulate the properties of cell walls, was found to be inhibited by the herbicide, which may be of significant value in understanding the effect of 2,4-D on the activity of T. harzianum. Expand


An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols.
The results establish that yeast contains at least two cis-IPTases, and indicate that the chain length of dolichols is determined primarily by the enzyme catalyzing the chain elongation stage of the biosynthetic process. Expand
Characterization of the Saccharomyces cerevisiae cis-prenyltransferase required for dolichyl phosphate biosynthesis.
The stereochemistry of addition of isoprene units by the prenyltransferase was shown to be cis by a comparison of the HPLC retention time for a pentadecaprenyl phosphate derived from the in vitro reaction product with that for an authentic mixture of alpha-cis- and alpha-trans-pentadecapreyl phosphates. Expand
Polyisoprenoids - Secondary metabolites or physiologically important superlipids?
A mini-review summarizes the results of recent studies on polyisoprenoids and shows a direct link between the dolichol biosynthetic pathway and congenital disorders of glycosylation (CDG). Expand
Identification of the lipid intermediate in yeast mannan biosynthesis.
The unsaponifiable lipid fraction of Saccharomyces cerevisiae contains a phosphorylated component which accepts a mannosyl residue from GDP-mannose and transfers it to growing mannan chains, which is the “lipid” intermediate in yeast cell wall biosynthesis. Expand
Dolichol phosphate mannose synthase from the filamentous fungus Trichoderma reesei belongs to the human and Schizosaccharomyces pombe class of the enzyme.
This work cloned a T.reesei cDNA that encodes a 243 amino acid protein whose amino acid sequence shows 67% and 65% identity, respectively, to the Schizosaccharomyces pombe and human DPM synthases, and which lacks the COOH-terminal hydrophobic domain characteristic of the SacCharomyces cerevisiae class of synthase. Expand
Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe.
It is found that Dol-P-Man synthase is essential in yeast and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raising the possibility that it could be exploited as a target for inhibitors of pathogenic eukaryotic microbes. Expand
Biosynthesis of dolichol phosphate by subcellular fractions from liver
It is surprising that very little attention has been given to the metabolism of dolichol, which is a generic name for long-chain polyprenols which are composed of an isoprenoid chain of 80 to 110 carbon atoms. Expand
Short-chain polyisoprenoids in the yeast Saccharomyces cerevisiae - New companions of the old guys.
The presence of additional short-chain length polyprenols - all-trans Pren-7 in three yeast strains was identified and simvastatin inhibited their biosynthesis. Expand
Structural basis for dolichylphosphate mannose biosynthesis
Three high-resolution crystal structures of archaeal DPMS from Pyrococcus furiosus are reported, in complex with nucleotide, donor, and glycolipid product to provide insight into the mechanism of Dol-P-Man synthesis. Expand
O-Glycosylation of Proteins by Membrane Fractions of Trichoderma reesei QM 9414
Mannosylation of endogenous proteins occurred at a lower rate with membranes isolated from glycerol-grown cells, suggesting a limitation of endogenous GDP-mannose and/or dolichol phosphate in glycerl-grown (i.e. catabolite-repressed) cells. Expand