Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe
Language English Country Netherlands Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
11690648
DOI
10.1016/s0167-4781(01)00301-3
PII: S0167478101003013
Knihovny.cz E-resources
- MeSH
- Cyclophilins metabolism MeSH
- Dictyostelium metabolism MeSH
- DNA-Binding Proteins genetics metabolism MeSH
- Gene Library MeSH
- Molecular Sequence Data MeSH
- Peptidylprolyl Isomerase genetics metabolism MeSH
- Protozoan Proteins * MeSH
- Schizosaccharomyces metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Cyclophilins MeSH
- DNA-Binding Proteins MeSH
- Peptidylprolyl Isomerase MeSH
- Protozoan Proteins * MeSH
- SNWA protein, Dictyostelium discoideum MeSH Browser
We screened the Dictyostelium discoideum two-hybrid cDNA library with the SNW/SKIP transcription coregulator SnwA and identified a novel cyclophilin CypE. Independently, the Schizosaccharomyces pombe cDNA library was screened with the SnwA ortholog Snw1 and the ortholog of CypE (named Cyp2) was found. Both cyclophilins bind the respective SNW protein in their autologous systems. The interaction was localized to the N-terminal part of SnwA as well as of Snw1. CypE was confirmed in vitro to be a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase. Remarkably, both SNW proteins bind the cyclophilins in a cyclosporin A independent manner, possibly serving as adaptors for these novel isomerases. These results are the first characterization of the members of a novel cyclophilin subfamily, which includes the human CGI-124/PPIL1 protein.
References provided by Crossref.org
GENBANK
AF215865, AF337536
