A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.
To facilitate folding and assembly of different proteins, chaperonin GroEL requires the presence of its helper protein GroES. Using a photochemical cross-linking approach, we show that GroES and newly synthesized pre-beta-lactamase (pre-beta lac) contact with each other only within the ternary complex with GroEL. Possibly owing to this contact GroES is able to directly influence the pre-beta lac/GroEL interaction. Furthermore, the cross-linking of pre-beta lac to GroES suggests that the binding of the protein ligands to GroEL occurs near the GroES binding site, known to be in the central hole space of GroEL.
Bochkareva
E S
ES
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Girshovich
A S
AS
D000227:Adenine Nucleotides / Q000378:metabolism; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D018835:Chaperonin 10; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D004792:Enzyme Precursors / Q000096:biosynthesis* / Q000302:isolation & purification; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D013462:Sulfur Radioisotopes; D014466:Ultraviolet Rays; D001618:beta-Lactamases / Q000096:biosynthesis* / Q000302:isolation & purification
D000227:Adenine Nucleotides; D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D004792:Enzyme Precursors; D006360:Heat-Shock Proteins; D013462:Sulfur Radioisotopes; C037640:pre-beta-lactamase; D001618:beta-Lactamases