Gene for a cyclophilin-type peptidyl-prolyl cis-trans isomerase from a halophilic archaeum, Halobacterium cutirubrum.
A gene encoding a cyclophilin (CyP)-type peptidyl prolyl cis-trans isomerase (PPIase) was cloned from a halophilic archaeum, Halobacterium cutirubrum DSM 669, and sequenced. Although amino-acid residues common to CyPs were conserved, an insertion that showed no homology to other CyPs was found in its N-terminal region. Sequence analysis revealed that the amino-acid sequence of this CyP was 40-45% identical to those of eukaryotes and Bacillus subtilis with high cyclosporin A sensitivity, but 27% identical to those of cyclosporin A-insensitive PPIases of Escherichia coli. The gene was also expressed in E. coli. The activity of purified recombinant CyP-type PPIase was stimulated by the addition of KCl, and was suppressed by cyclosporin A.
Iida
T
T
Marine Biotechnology Institute, Kamaishi Laboratories, Iwate, Japan. tiida@kamaishi.mbio.co.jp
Furutani
M
M
Iwabuchi
T
T
Maruyama
T
T
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D019641:DNA, Archaeal; D004926:Escherichia coli; D019766:Genes, Archaeal; D006217:Halobacterium / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D019641:DNA, Archaeal; D019696:Peptidylprolyl Isomerase