Crosstalk of Prolyl Isomerases, Pin1/Ess1, and Cyclophilin A

• Published in: Biochemical and biophysical research communications Vol. 289; no. 1; pp. 181 - 190
• Main Authors: Fujimori, Fumihiro, Gunji, Wataru, Kikuchi, Junko, Mogi, Tomoko, Ohashi, Yoko, Makino, Tohru, Oyama, Akira, Okuhara, Koji, Uchida, Takafumi, Murakami, Yasufumi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.11.2001
• Subjects: Base Sequence; cell cycle; Cell Cycle - physiology; cyclophilin A; Cyclophilin A - genetics; Cyclophilin A - metabolism; DNA, Fungal - genetics; Ess1; ess1 gene; Ess1 protein; G1 Phase - physiology; Gene Deletion; Gene Expression; Genes, Fungal; microarray; NIMA-Interacting Peptidylprolyl Isomerase; Oligonucleotide Array Sequence Analysis; Peptidylprolyl Isomerase - genetics; Peptidylprolyl Isomerase - metabolism; peptydyl-prolyl cis/trans isomerase; Phenotype; Pin1; Pin1 protein; PPIase; RNA, Fungal - genetics; RNA, Fungal - metabolism; RNA, Messenger - genetics; RNA, Messenger - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - cytology; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins; microarray; cell cycle; cyclophilin A; PPIase; Pin1; peptydyl-prolyl cis/trans isomerase; Ess1
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.2001.5925

Previous studies have indicated that Ess1/Pin1, a gene in the parvulin family of peptidyl-prolyl isomerases (PPIases), plays an important role in regulating the G2/M transition of the cell cycle by binding cell-cycle-regulating proteins in eukaryotic cells. Although the ess1 gene has been considered to be essential in yeast, we have isolated viable ess1 deletion mutants and demonstrated, via analysis of yeast gene expression profiles using microarray techniques, a novel regulatory role for ESS1 in the G1 phase. Although the overall expression profiles in the tested strains (C110-1, W303, S288c, and RAY-3AD) were similar, marked changes were detected for a number of genes involved in the molecular action of ESS1. Among these, the expression levels of a cyclophilin A gene, also a member of the PPIase family, increased in the ess1 null mutant derived from C110-1. Subsequent treatment with cyclosporin A significantly retarded growth, which suggests that ESS1 and cyclophilin A are functionally linked in yeast cells and play important roles at the G1 phase of the cell cycle.