Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region.

@article{Vai1991IsolationAD,
  title={Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region.},
  author={Marina Vai and Evelina Gatti and Emanuela Lacan{\'a} and Laura Popolo and Lilia Alberghina},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 19},
  pages={12242-8}
}
gp115 is a N- and O-glycosylated protein of Saccharomyces cerevisiae. It is also modified by addition of glycosylphosphatidylinositol, which anchors the protein to the plasma membrane. The gene encoding gp115 (GGP1) has been cloned by a two-step procedure. By an immunoscreening of a yeast genomic DNA library in the expression vector lambda gt11, a 3'-terminal 0.9-kilobase portion of the gene has been isolated and then used as a molecular probe to screen a yeast genomic DNA library in YEp24. In… CONTINUE READING

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The predicted amino acid sequence of gp115 shows 10 sequons for N - glycosylation and a high proportion of serine - threonine residues ( 22% ) that could provide several sites for O - glycosylation .
The predicted amino acid sequence of gp115 shows 10 sequons for N - glycosylation and a high proportion of serine - threonine residues ( 22% ) that could provide several sites for O - glycosylation .
Its identity with the gp115 gene has been confirmed by gene disruption , which has also indicated that the function of gp115 is not essential for cell viability .
Its identity with the gp115 gene has been confirmed by gene disruption , which has also indicated that the function of gp115 is not essential for cell viability .
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