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PMID:8543034

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Citation

Gentzsch, M, Immervoll, T and Tanner, W (1995) Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer. FEBS Lett. 377:128-30

Abstract

The protein O-mannosyltransferases Pmt1p and Pmt2p are catalyzing the O-glycosylation of serine and threonine residues in the endoplasmic reticulum of yeast. Deletion of each of these proteins by disruption of the corresponding gene leads to a dramatic decrease of mannosyltransferase activity in vitro. With an anti-Pmt1p immunoaffinity column a complex of Pmt1p and a second protein was purified; this protein turned out to be Pmt2p. Overexpression of Pmt1p or Pmt2p, respectively, does not increase mannosyltransferase activity in vitro. Overexpression of both mannosyltransferases together, however, raises in vitro activity threefold. These data indicate that Pmt1p and Pmt2p function as a complex catalyzing protein O-glycosylation in yeast.

Links

PubMed

Keywords

Amino Acid Sequence; Fungal Proteins/metabolism; Glycosylation; Isoenzymes/metabolism; Mannosyltransferases/genetics; Mannosyltransferases/isolation & purification; Mannosyltransferases/metabolism; Molecular Sequence Data; Saccharomyces cerevisiae/isolation & purification; Saccharomyces cerevisiae/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:PMT2

part_of

GO:0097582: dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex

ECO:0000353: physical interaction evidence used in manual assertion

SGD:S000002253

C

Seeded From UniProt

complete

YEAST:PMT2

enables

GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

YEAST:PMT2

enables

GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity

ECO:0000316: genetic interaction evidence used in manual assertion

SGD:S000002253

F

Seeded From UniProt

complete

YEAST:PMT2

involved_in

GO:0035269: protein O-linked mannosylation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:PMT2

involved_in

GO:0035269: protein O-linked mannosylation

ECO:0000316: genetic interaction evidence used in manual assertion

SGD:S000002253

P

Seeded From UniProt

complete

YEAST:PMT1

part_of

GO:0097582: dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex

ECO:0000353: physical interaction evidence used in manual assertion

SGD:S000000021

C

Seeded From UniProt

complete

YEAST:PMT1

enables

GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

YEAST:PMT1

enables

GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

YEAST:PMT1

enables

GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity

ECO:0000316: genetic interaction evidence used in manual assertion

SGD:S000000021

F

Seeded From UniProt

complete

YEAST:PMT1

involved_in

GO:0035269: protein O-linked mannosylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:PMT1

involved_in

GO:0035269: protein O-linked mannosylation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:PMT1

involved_in

GO:0035269: protein O-linked mannosylation

ECO:0000316: genetic interaction evidence used in manual assertion

SGD:S000000021

P

Seeded From UniProt

complete


See also

References

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