cDNA encoding protein 0-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2

Anna Zakrzewska, Andrzej Migdalski, Markku Saloheimo, Merja Penttilä, Grazyna Palamarczyk, Joanna Kruszewska (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

Abstract

O-Mannosylation is suggested to be essential for protein secretion in Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is transferred to a serine or threonine hydroxyl group of the protein from dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the present work, the characterisation of the pmt1 cDNA from T. reesei is reported. Sequence analysis of the predicted protein revealed the highest similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces cerevisiae. In contrast, expression of the T. reesei cDNA in various S. cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.
Original languageEnglish
Pages (from-to)11-16
JournalCurrent Genetics
Volume43
Issue number1
DOIs
Publication statusPublished - 2003
MoE publication typeA1 Journal article-refereed

Keywords

  • pmt gene
  • Protein glycosylation
  • 0-Mannosylation
  • Secretion

Fingerprint Dive into the research topics of 'cDNA encoding protein 0-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2'. Together they form a unique fingerprint.

  • Cite this