Related Experiment Video
Updated: Jun 26, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Functional characterization of the DnaK chaperone system from the archaeon Methanothermobacter thermautotrophicus
Simone L Popp1, Jochen Reinstein
1Max-Planck-Institute for Medical Research, Department of Biomolecular Mechanisms, Heidelberg, Germany.
Abstract:
We characterized the biochemical and functional properties of the DnaK system from the archaeon Methanothermobacter thermautotrophicus DeltaH. In contrast to the eubacterial chaperone components the archaeal Hsp70 system shows thermal transitions only slightly above the optimal environmental temperature (65 degrees C). Nevertheless, it prevents aggregation of luciferase in the physiological temperature range of the organism, but is also fully functional at 30 degrees C in luciferase refolding. Additionally, GrpE(M.th.) and DnaJ(M.th.) substitute their eubacterial counterparts whereas DnaK(M.th.) is only functional with its native cochaperones which could be attributed to a functional specialization of the eubacterial chaperones during evolution.
Related Concept Videos
Diversity of Archaea III
Nucleoid
Diversity of Archaea IV
Bacterial Protein Maturation
Molecular Chaperones and Protein Folding
The...
Diversity of Archaea I

