Characterization of the cyclophilin of Trichophyton mentagrophytes.
A genetic approach to cyclophilins in a dermatophyte, Trichophyton mentagrophytes, was carried out. The nucleotide and deduced amino acid sequences of the cyclophilin of T. mentagrophytes shared about 70% sequence similarity with those of Schizosaccharomyces pombe, Saccharomyces cerevisiae and Candida albicans. However, the first 21 amino acid and the C-terminal amino acid regions of 188 to 226 of the T. mentagrophytes cyclophilin were distinct from those of the other fungal cyclophilins. The recombinant glutathione S-transferase (GST)-T. mentagrophytes cyclophilin fusion protein produced by Escherichia coli was purified. The protease digest of the fusion protein had a molecular weight of about 13 kDa and peptidyl-prolyl cis-trans isomerase (PPI) activity. This digest protein from T. mentagrophytes was confirmed to be cyclophilin by proving PPI activity.
Kano
R
R
Department of Pathobiology, Nihon University School of Veterinary Medicine, Fujisawa, Kanagawa, Japan. kano@brs.nihon-u.ac.jp
Nakamura
Y
Y
Watanabe
S
S
Tsujimoto
H
H
Hasegawa
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D004271:DNA, Fungal; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014249:Trichophyton / Q000201:enzymology* / Q000235:genetics
D004271:DNA, Fungal; D019696:Peptidylprolyl Isomerase