Streptomyces lividans possesses a GroEL-like chaperonin.
Streptomyces lividans grown at 45 degrees 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 Escherichia coli and Bacillus subtilus and shows immunological cross-reaction with serum raised against GroEL 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 symmetries as previously described in E. coli and B. subtilis.
Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain.
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D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000648:ultrastructure; D018834:Chaperonin 60; D018833:Chaperonins; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000648:ultrastructure; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification; D011506:Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000648:ultrastructure; D013302:Streptomyces / Q000737:chemistry* / Q000648:ultrastructure
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D010455:Peptides; D011506:Proteins; D018833:Chaperonins