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The purine‐cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product
Author(s) -
Weber E.,
Rodriguez C.,
Chevallier M. R.,
Jund R.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00627.x
Subject(s) - biology , permease , gene , gene product , saccharomyces cerevisiae , hspa2 , gps2 , hspa9 , mutant , gene cluster , syt1 , akt1s1 , protein primary structure , biochemistry , genetics , peptide sequence , microbiology and biotechnology , gene expression
Summary A 2.1 kb DNA segment carrying the purine‐cytosine permease gene ( FCY2 ) of Saccharomyces cerevisiae was sequenced, the primary structure of the protein (533 amino acids) deduced and a folding pattern in the membrane is proposed for the permease protein. Expression of the FCY2 gene product requires a functional secretory pathway and is reduced in mnn9 , a mutant strain deficient in outer chain glycosylation. The FCY2 gene was mapped on the right arm of chromosome V close to the HIS1 gene.