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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1992-4-29
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0749-503X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
7
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
971-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:1803821-Amino Acid Isomerases,
pubmed-meshheading:1803821-Amino Acid Sequence,
pubmed-meshheading:1803821-Animals,
pubmed-meshheading:1803821-Base Sequence,
pubmed-meshheading:1803821-Blotting, Northern,
pubmed-meshheading:1803821-Blotting, Southern,
pubmed-meshheading:1803821-Carrier Proteins,
pubmed-meshheading:1803821-Cloning, Molecular,
pubmed-meshheading:1803821-Cyclosporins,
pubmed-meshheading:1803821-DNA, Fungal,
pubmed-meshheading:1803821-Drosophila melanogaster,
pubmed-meshheading:1803821-Escherichia coli,
pubmed-meshheading:1803821-Genes, Fungal,
pubmed-meshheading:1803821-Molecular Sequence Data,
pubmed-meshheading:1803821-Open Reading Frames,
pubmed-meshheading:1803821-Peptidylprolyl Isomerase,
pubmed-meshheading:1803821-Restriction Mapping,
pubmed-meshheading:1803821-Saccharomyces cerevisiae
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae.
|
| pubmed:affiliation |
Centro de Biología Molecular (C.S.I.C./U.A.M.), Universidad Autónoma, Madrid, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|