Journal
FEBS LETTERS
Volume 583, Issue 3, Pages 573-578Publisher
WILEY
DOI: 10.1016/j.febslet.2008.12.062
Keywords
DnaK; Chaperone; Archaea; ATPase activity; Luciferase refolding; Methanothermobacter thermautotrophicus; Delta H
Ask authors/readers for more resources
We characterized the biochemical and functional properties of the DnaK system from the archaeon Methanothermobacter thermautotrophicus Delta H. 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. (c) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available