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

Fingerprint

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

Keywords

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

Cite this

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title = "cDNA encoding protein 0-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.",
keywords = "pmt gene, Protein glycosylation, 0-Mannosylation, Secretion",
author = "Anna Zakrzewska and Andrzej Migdalski and Markku Saloheimo and Merja Penttil{\"a} and Grazyna Palamarczyk and Joanna Kruszewska",
year = "2003",
doi = "10.1007/s00294-003-0368-5",
language = "English",
volume = "43",
pages = "11--16",
journal = "Current Genetics",
issn = "0172-8083",
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}

cDNA encoding protein 0-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2. / Zakrzewska, Anna; Migdalski, Andrzej; Saloheimo, Markku; Penttilä, Merja; Palamarczyk, Grazyna; Kruszewska, Joanna (Corresponding Author).

In: Current Genetics, Vol. 43, No. 1, 2003, p. 11-16.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - cDNA encoding protein 0-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2

AU - Zakrzewska, Anna

AU - Migdalski, Andrzej

AU - Saloheimo, Markku

AU - Penttilä, Merja

AU - Palamarczyk, Grazyna

AU - Kruszewska, Joanna

PY - 2003

Y1 - 2003

N2 - 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.

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.

KW - pmt gene

KW - Protein glycosylation

KW - 0-Mannosylation

KW - Secretion

U2 - 10.1007/s00294-003-0368-5

DO - 10.1007/s00294-003-0368-5

M3 - Article

VL - 43

SP - 11

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JO - Current Genetics

JF - Current Genetics

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