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

International Journal of Biological Macromolecules
Vineeta KaushikManisha Goel

Abstract

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. In the present work, we characterize in detail a cyclophilin from the archaea, Methanobrevibacter ruminantium (MrCyp). We explore the functional and structural characteristics of MrCyp using various biophysical techniques. MrCyp exhibits both the PPIase and aggregation prevention activity. Analysis of folding/unfolding data and measurement of ∆GNUH2O and Tm suggest that the protein is thermodynamically stable. MrCyp helps in increasing cell viability of E. coli cells. These features imply that MrCyp could be a promising candidate for co-expression mediate...Continue Reading

Citations

Dec 5, 2020·International Journal of Biological Macromolecules·Sefli Sri Wahyu EffendiI-Son Ng
Feb 10, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Archana SharmaManisha Goel
Apr 10, 2020·Protein Expression and Purification·Selvakumari UlagesanYoun-Hee Choi
Oct 26, 2021·Frontiers in Microbiology· AnchalManisha Goel

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