Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
11690648
DOI
10.1016/s0167-4781(01)00301-3
PII: S0167478101003013
Knihovny.cz E-zdroje
- MeSH
- cyklofiliny metabolismus MeSH
- Dictyostelium metabolismus MeSH
- DNA vazebné proteiny genetika metabolismus MeSH
- genová knihovna MeSH
- molekulární sekvence - údaje MeSH
- peptidylprolylisomerasa genetika metabolismus MeSH
- protozoální proteiny * MeSH
- Schizosaccharomyces metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- cyklofiliny MeSH
- DNA vazebné proteiny MeSH
- peptidylprolylisomerasa MeSH
- protozoální proteiny * MeSH
- SNWA protein, Dictyostelium discoideum MeSH Prohlížeč
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.
Citace poskytuje Crossref.org
GENBANK
AF215865, AF337536
