Evidence of interaction of phage P22 tailspike protein with DnaJ during translational folding

Cited 0 time in scopus
Metadata Downloads
Title
Evidence of interaction of phage P22 tailspike protein with DnaJ during translational folding
Author(s)
Sang Chul Lee; M H Yu
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 14, no. 1, pp. 162-166
Publication Year
2004
Abstract
Phage P22 tailspike is a thermostable homotrimeric protein, and temperature-sensitive folding (tsf) and global suppressor mutations affect its folding yields at elevated temperatures. We earlier suggested that the folding of the tailspike protein in Escherichia coli requires an unidentified molecular chaperone. Accordingly, in the present study, the interactions of purified DnaK, DnaJ, and GrpE heat-shock proteins with the tailspike protein were investigated during the translation and folding of the protein. The cotranslational addition of DnaJ to the tailspike protein resulted in the arrest of folding, when Dnak and GrpE were missing. However, the presence of DnaK, DnaJ, and GrpE had no effect on the folding yield of the tailspike protein, thus, providing evidence for the binding of the nascent tailspike protein with DnaJ protein, a member of DnaK chaperoning cycle.
Keyword
bacterophage P22DnaJmolecular chaperoneprotein foldingtailspike protein
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.