Journal
BMB REPORTS
Volume 44, Issue 12, Pages 816-820Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2011.44.12.816
Keywords
Dimer; Mitochondrial sHSP; Molecular chaperone; NtHSP24.6; Substrate range
Categories
Funding
- National Research Foundation of Korea (NRF) [2008-005-J00202]
- Ministry of Education, Science and Technology, Korea
- Ministry for Agriculture, Forestry and Fisheries of Korea
- National Research Foundation of Korea [2008-005-J00202] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
There is a broad range of different small heat shock proteins (sHSPs) that have diverse structural and functional characteristics. To better understand the functional role of mitochondria! sHSP, NtHSP24.6 was expressed in Escherichia coli with a hexahistidine tag and purified. The protein was analyzed by non-denaturing PAGE, chemical cross-linking and size exclusion chromatography and the H(6)NtHSP24.6 protein was found to form a dimer in solution. The in vitro functional analysis of H(6)NtHSP24.6 using firefly luciferase and citrate synthase demonstrated that this protein displays typical molecular chaperone activity. When cell lysates of E. coli were heated after the addition of H(6)NtHSP24.6, a broad range of proteins from 10 to 160 kD in size remained in the soluble state. These results suggest that NtHSP24.6 forms a dimer and can function as a molecular chaperone to protect a diverse range of proteins from thermal aggregation. [BMB reports 2011; 44(12): 816-820]
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