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Streptomycetes possess peptidyl‐prolyl cis‐trans isomerases that strongly resemble cyclophilins from eukaryotic organisms
Author(s) -
Pahl Andreas,
Ühlein Monika,
Bang Holger,
Schlumbohm Wilhelm,
Keller Ullrich
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01790.x
Subject(s) - biology , cis trans isomerases , isomerase , peptidylprolyl isomerase , fkbp , pin1 , trans acting , prolyl isomerase , biochemistry , microbiology and biotechnology , enzyme , gene , mutant
Summary A functionally active 17.5 kDa peptidyl‐prolyl cis‐trans isomerase was purified to homogeneity from Streptomyces chrysomallus , a Gram‐positive filamentous bacterium. Characterization of the enzyme revealed inhibition and binding characteristics, against the immunsuppressive drug cyclosporin A, which were similar to cyclophilins from eukaryotes such as mammals, plants, fungi and yeasts, but different from those of cyclophilins from enterobacteria such as Escherichia coli. The amino acid sequence of the S. chrysomallus cyclophilin, as deduced from the gene sequence, revealed a striking degree of amino acid sequence identity with the corresponding 17 kDa proteins of humans (66%), Neurospora (70%) and yeast (69%). Comparison with cyclophilin sequences from the Gram‐negative enterobacteria revealed much iess homoiogy (25% identity with E. coli b, 23% identity with E. coli a). Cyclophilin was detected in each of the four other Streptomyces species tested. The cyclophilins from the various streptomycetes differed in size, varying between 17 and 20.5 kDa. The cyclophilins were abundant in the Streptomyces cells, and present throughout growth.