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 language | English |
---|---|
Pages (from-to) | 445-450 |
Number of pages | 6 |
Journal | Current Genetics |
Volume | 33 |
Issue number | 6 |
DOIs | |
Publication status | Published - 1 Jan 1998 |
MoE publication type | A1 Journal article-refereed |
Keywords
- dpm1 mutant
- Glycosylation
- GTP:α-D-mannose-1-phosphate guanyltransferase
- mpg1 gene
- S. cerevisiae
- Trichoderma reesei