Open AccessIdentification and characterization of GroEL and DnaK homologues in Thiobacillus ferrooxidans
Author(s) -
Varela Patricia,
Jerez Carlos A.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05505.x
Subject(s) - groel , escherichia coli , chaperonin , gel electrophoresis , blot , biology , microbiology and biotechnology , polyacrylamide gel electrophoresis , biochemistry , heat shock protein , hsp60 , chemistry , hsp70 , protein folding , enzyme , gene
The major heat shock proteins from Thiobacillus ferrooxidans were identified as DnaK and GroEL equivalents by Western blotting and analysis of the N‐terminal amino acid sequence of spots isolated from dried 2‐D polyacrylamide electrophoresis gels. The T. ferrooxidans chaperonins showed 70% and 80% identity with the Escherichia coli GroEL and DnaK, respectively. By using electrophoresis with a transverse pore gradient of cross‐linked polyacrylamide and nondenaturing conditions followed by Western blotting, we found that the GroEL proteins from both bacteria formed a 14‐mer, whereas E. coli DnaK protein existed partially as a dimer and the T. ferrooxidans DnaK‐equivalent showed only a monomeric nature under our experimental conditions.