Open AccessStreptomyces lividans possesses a GroEL‐like chaperonin
Author(s) -
Marco Sergio,
Parro Víctor,
Carrascosa JoséL.,
Mellado Rafael P.
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.tb05078.x
Subject(s) - groel , chaperonin , bacillus subtilis , biology , streptomyces , escherichia coli , groes , heat shock protein , streptomycetaceae , bacillaceae , chaperone (clinical) , biochemistry , actinomycetales , bacillales , protein folding , microbiology and biotechnology , bacteria , genetics , gene , medicine , pathology
Streptomyces lividans grown at 45°C produces a GroEL‐like chaperonin. This protein is specifically synthesized in bacterial cell cultures upon heat shock induction. It has a similar size (62 kDa) to the GroEL‐like proteins from Eschirichia coli and Bacillus subtilus and shows immunological cross‐reaction with serum raised against GroEL like from E. coli . The S. lividans 62‐kDa protein assembles into oligomers around 20S that show a morphology consistent with a barrel showing six‐fold and seven‐fold symmetrues as previously described in E. coli and B. subtilis .