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

Fingerprint Dive into the research topics of 'Isolation of a Trichoderma reesei cDNA encoding GTP: α-d-mannose-1-phosphate guanyltransferase involved in early steps of protein glycosylation'. Together they form a unique fingerprint.

  • Cite this