Biophysical and biochemical characterization of a thermostable archaeal cyclophilin from Methanobrevibacter ruminantium

摘要

The archaeal protein folding machinery is quite similar to that found in eukaryotes, especially in terms of shared components like chaperones. Cyclophilins are chaperones found in both eukaryotes and archaea, which catalyze the reversible cis-trans isomerization around peptidyl-prolyl imide bond (PPIase activity). Eukaryotes possess multiple cyclophilin genes, many of which have acquired divergent functions. Archaea, having a single copy of this gene, may help better in comprehending the role of cyclophilins in maintaining cellular proteostasis. However, no cyclophilin homologs from archaea have been characterized as yet, limiting comparison with their eukaryotic counterparts.