TheSchizosaccharomyces pombeGPI8 gene complements aSaccharomyces cerevisiaeGPI8 anchoring mutant
Autor: | Ralph T. Schwarz, Mamdouh H. Kedees, Hosam Shams-Eldin, Andreas Hübel, Volker Eckert, Nahid Azzouz, Thomas Blaschke |
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Rok vydání: | 2000 |
Předmět: |
chemistry.chemical_classification
biology Mutant Saccharomyces cerevisiae Nucleic acid sequence Anchoring Bioengineering Cell Surface Proteins biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Amino acid chemistry Schizosaccharomyces pombe Genetics Gene Biotechnology |
Zdroj: | Yeast. 18:33-39 |
ISSN: | 1097-0061 0749-503X |
DOI: | 10.1002/1097-0061(200101)18:1<33::aid-yea648>3.0.co;2-z |
Popis: | 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. The nucleotide sequence data reported in this paper appears in the EMBL Data Bank nucleotide sequence database with Accession No. AJ250428. Copyright © 2000 John Wiley & Sons, Ltd. |
Databáze: | OpenAIRE |
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