cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei

functional equivalence to Saccharomyces cerevisiae PMT2

Anna Zakrzewska, Andrzej Migdalski, Markku Saloheimo, Merja E. Penttila, Grazyna Palamarczyk, Joanna S. Kruszewska

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)

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
Number of pages6
JournalCurrent Genetics
Volume43
Issue number1
Publication statusPublished - 1 Apr 2003
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Saccharomyces cerevisiae
Fungi
Complementary DNA
Fungal Proteins
Schizosaccharomyces
Protein Sequence Analysis
Threonine
Glycosylation
Hydroxyl Radical
Serine
Proteins
Enzymes
Genes
protein O-mannosyltransferase

Keywords

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

Cite this

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title = "cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei: functional equivalence to Saccharomyces cerevisiae PMT2",
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.",
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cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei : functional equivalence to Saccharomyces cerevisiae PMT2. / Zakrzewska, Anna; Migdalski, Andrzej; Saloheimo, Markku; Penttila, Merja E.; Palamarczyk, Grazyna; Kruszewska, Joanna S.

In: Current Genetics, Vol. 43, No. 1, 01.04.2003, p. 11-16.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei

T2 - functional equivalence to Saccharomyces cerevisiae PMT2

AU - Zakrzewska, Anna

AU - Migdalski, Andrzej

AU - Saloheimo, Markku

AU - Penttila, Merja E.

AU - Palamarczyk, Grazyna

AU - Kruszewska, Joanna S.

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AB - 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.

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