Isolation of a Trichoderma reesei cDNA encoding GTP: α-d-mannose-1-phosphate guanyltransferase involved in early steps of protein glycosylation

Joanna S. Kruszewska, Markku Saloheimo, Merja Penttilä, Grazyna Palamarczyk

    Research output: Contribution to journalArticleScientificpeer-review

    16 Citations (Scopus)

    Abstract

    A cDNA coding for GTP:α-D-mannose-1-phosphate guanyltransferase (MPG1 transferase) (EC 2.7.7.13) was isolated from a cDNA library of the Trichoderma reesei RutC-30 strain by suppression of the yeast Saccharomyces cerevisiae mutation in the DPM1 gene encoding mannosylphosphodolichol (MPD) synthase. The nucleotide sequence of the 1.6 kb-long cDNA revealed an ORF which encodes a protein of 364 amino acids. Sequence comparisons demonstrate 70% identity with the S. cerevisiae guanyl transferase gene (MPG1) and 75% identity with the Schizosaccharomyces pombe homologue. No similarity was found with the MPD synthase encoded by the S. cerevisiae DPM1 gene. 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. Simultaneously, a significant increase in MPG transferase activity, as compared with the wild-type yeast, was observed in cellular extracts when the mpg1 cDNA from Trichoderma was expressed in the S. cerevisiae dpm1-6 mutant.

    Original languageEnglish
    Pages (from-to)445-450
    Number of pages6
    JournalCurrent Genetics
    Volume33
    Issue number6
    DOIs
    Publication statusPublished - 1 Jan 1998
    MoE publication typeA1 Journal article-refereed

    Keywords

    • dpm1 mutant
    • Glycosylation
    • GTP:α-D-mannose-1-phosphate guanyltransferase
    • mpg1 gene
    • S. cerevisiae
    • Trichoderma reesei

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