Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe

• Published in: Biochimica et biophysica acta Vol. 1521; no. 1; pp. 146 - 151
• Main Authors: Skružný, Michal, Ambrozková, Monika, Fuková, Iva, Martı́nková, Kateřina, Blahůšková, Anna, Hamplová, Ludmila, Půta, František, Folk, Petr
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 31-10-2001
• Subjects: Amino Acid Sequence; Animals; Cyclophilin; Cyclophilins - metabolism; Dictyostelium - metabolism; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Gene Library; Molecular Sequence Data; Peptidylprolyl Isomerase - genetics; Peptidylprolyl Isomerase - metabolism; Prolyl isomerase; Protozoan Proteins; Schizosaccharomyces - metabolism; Sequence Alignment; SNW coregulator; Yeast two-hybrid analysis; GFP, green fluorescent protein; PPIase, peptidyl-prolyl cis-trans isomerase; Yeast two-hybrid analysis; Cyclophilin; SNW coregulator; CsA, cyclosporin A; Prolyl isomerase
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/S0167-4781(01)00301-3

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.