Open AccessIdentification and characterization of a GroEL homologue in Rhodobacter sphaeroides
Author(s) -
Watson G.M.F.,
Mann N.H.,
MacDonald G.A.,
Dunbar B.
Publication year - 1990
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.1574-6968.1990.tb03915.x
Subject(s) - groel , rhodobacter sphaeroides , chaperonin , protein subunit , biochemistry , biology , escherichia coli , rhodospirillales , rhodospirillaceae , antiserum , peptide sequence , microbiology and biotechnology , gel electrophoresis , polyacrylamide gel electrophoresis , protein folding , genetics , antibody , enzyme , gene , photosynthesis
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 M r 670 000 which is composed of a monomer of M r 58 000. Antisera raised against the M r 58 000 polypeptide have been shown to cross‐react with GroEL and the α subunit of the pea plastid chaperonin. The N‐terminal amino acid sequence of the M r 58 000 polypeptide is identical to that of GroEL at 15 of 19 residues and is also closely related to the α subunit of the pea plastid chaperonin, though less so that the β subunit.