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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Feb 15;89(4):1164–1168. doi: 10.1073/pnas.89.4.1164

Neisseria meningitidis encodes an FK506-inhibitable rotamase.

B A Sampson 1, E C Gotschlich 1
PMCID: PMC48409  PMID: 1371354

Abstract

Eukaryotic peptidyl-prolyl cis-trans isomerases (rotamases) fall into two classes, the cyclophilins inhibited by cyclosporin A and the FK506-binding proteins inhibited by the macrolide antibiotic FK506. In prokaryotes homologs of cyclophilins have been identified and found to have rotamase activity. Sequence similarities have been noted between FK506-binding proteins and gene products in a number of bacterial species, but whether these bacterial proteins have rotamase activity is not known. Using the polymerase chain reaction, we have cloned and sequenced a homolog of an FK506-binding protein from Neisseria meningitidis and expressed the gene product as a fusion protein with maltose-binding protein. The fusion protein was purified by affinity chromatography. By measuring the rate of chymotrypsin cleavage of the substrate succinyl-Ala-Ala-Pro-Phe p-nitroanilide, we found that the fusion protein had rotamase activity comparable to that of human FK506-binding protein. This rotamase activity was inhibited by FK506.

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Selected References

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