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The nucleotide sequence of a third cyclophilin‐homologous gene from Saccharomyces cerevisiae
Author(s) -
Franco L.,
Jiménez A.,
Demolder J.,
Molemans F.,
Fiers W.,
Contreras R.
Publication year - 1991
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320070909
Subject(s) - biology , cyclophilin , transmembrane domain , saccharomyces cerevisiae , peptide sequence , transmembrane protein , nucleic acid sequence , gene , open reading frame , signal peptide , endoplasmic reticulum , amino acid , genetics , biochemistry , receptor
The nucleotide sequence of a 1558 bp DNA fragment from the right arm of chromosome III of Saccharomyces cerevisiae contains an open reading frame of 954 nucleotides with coding potential for a protein with high similarity to the ubiquitous cyclophilins which are both peptidyl‐prolyl cis ‐ trans isomerases and cyclosporin A‐binding proteins. It should, therefore, represent the third gene ( SCC3 ) of this kind from S. cerevisiae . SCC3 is present in a single copy in the genome of S. cerevisiae and results in a constitutively expressed 1·2 kb transcript during cell growth. Its putative protein product (Scc3) contains two hydrophobic cores, one at the amino terminal, 20 amino acids long, which could serve as a signal peptide, and the other one at the carboxyl end with a structure similar to a transmembrane helix. These findings suggest that Scc3 could be a secretory or, more likely, a transmembrane protein. The only cyclophilin with similar structure to that of Scc3 is ninaA from Drosophila melanogaster , a transmembrane protein which seems to be implicated in the correct folding and/or intercalation of rhodopsin in the endoplasmic reticulum of the fly photoreceptors (Stamnes, M. A. et al. , Cell 65 , 219–227, 1991). In addition, the amino and the carboxy regions of Scc3 and ninaA share a significant level of homology, which suggests that they have a similar function, albeit for different target proteins.