Identification and characterization of a GroEL homologue in Rhodobacter sphaeroides.
A protein closely related to the Escherichia coli GroEL protein has been isolated from Rhodobacter sphaeroides. Native and SDS-polyacrylamide gel electrophoresis of this protein have shown that it is present in the cell as a multimeric complex of Mr 670,000 which is composed of a monomer of Mr 58,000. Antisera raised against the Mr 58,000 polypeptide have been shown to cross-react with GroEL and the alpha subunit of the pea plastid chaperonin. The N-terminal amino acid sequence of the Mr 58,000 polypeptide is identical to that of GroEL at 15 of 19 residues and is also closely related to the alpha subunit of the pea plastid chaperonin, though less so to the beta subunit.
Watson
G M
GM
Department of Biological Sciences, University of Warwick, Coventry, U.K.
Mann
N H
NH
MacDonald
G A
GA
Dunbar
B
B
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics / Q000276:immunology; D018834:Chaperonin 60; D018833:Chaperonins; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000032:analysis; D006360:Heat-Shock Proteins / Q000032:analysis* / Q000235:genetics / Q000276:immunology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010946:Plants, Medicinal; D011506:Proteins / Q000235:genetics; D012242:Rhodobacter sphaeroides / Q000032:analysis* / Q000235:genetics / Q000276:immunology; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D011506:Proteins; D018833:Chaperonins