The C-terminal sequence of the chaperonin GroES is required for oligomerization.
The Escherichia coli protein GroES is a co-chaperonin that is able to assist GroEL in the refolding of proteins. GroES is a heptamer of seven identical subunits. Recent work has focused on the structural aspects of GroES. We have investigated the role of the C-terminal portion of GroES on its oligomerization. Limited proteolysis of GroES by carboxypeptidase Y gives a product in which the C-terminal 7 amino acid residues have been removed. Sedimentation velocity analysis reveals that the truncated form of GroES is unable to reassemble. The results presented here implicate the C-terminal sequence in intermonomer actions within the GroES oligomer. In addition, this work provides experimental verification of predictions implied in the recent x-ray determination of the GroES structure (Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L. M., and Deisenhofer, J. Nature, in press).
Seale
J W
JW
Department of Biochemistry, University of Texas Health Sciences Center, San Antonio 78240-7760, USA.
Horowitz
P M
PM
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000378:metabolism; D043402:Cathepsin A; D018835:Chaperonin 10 / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D017510:Protein Folding
D018835:Chaperonin 10; D046911:Macromolecular Substances; D010446:Peptide Fragments; D002268:Carboxypeptidases; D043402:Cathepsin A