The Schizosaccharomyces pombe GPI8 gene complements a Saccharomyces cerevisiae GPI8 anchoring mutant
The final step in glycosylphosphatidylinositol (GPI) anchoring of cell surface proteins consists of a transamidation reaction, in which preassembled GPI donors are substituted for C-terminal signal sequences in nascent polypeptides. The Saccharomyces cerevisiae GPI8 gene (ScGPI8) encodes a protein w...
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Veröffentlicht in: | Yeast (Chichester, England) England), 2001-01, Vol.18 (1), p.33-39 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The final step in glycosylphosphatidylinositol (GPI) anchoring of cell surface proteins consists of a transamidation reaction, in which preassembled GPI donors are substituted for C-terminal signal sequences in nascent polypeptides. The Saccharomyces cerevisiae GPI8 gene (ScGPI8) encodes a protein which is involved in the GPI transamidation reaction. We have cloned and isolated the Schizosaccharomyces pombe GPI8 homologous gene (SpGPI8). The SpGPI8 gene encodes a protein of 411 amino acids with a calculated molecular weight of about 47 kDa. It shows 53.5% identity with the ScGPI8 and complements a S. cerevisiae GPI8 anchoring mutant. |
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ISSN: | 0749-503X |
DOI: | 10.1002/1097-0061(200101)18:1<33::AID-YEA648>3.0.CO;2-Z |