Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

Abstract

It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which may prevent or reverse the formation of misfolded structures or promote the correct assembly of oligomeric proteins or post-translational secretion. Using a photocross-linking approach, we have identified the 20S heat-shock GroEL protein as the major cytosolic component which forms a complex with the unfolded newly synthesized pre-beta-lactamase or chloramphenicol acetyltransferase in Escherichia coli. Dissociation of these complexes is ATP-dependent. The unfolded state of pre-beta-lactamase, maintained by the transient interaction with GroEL, may be essential for the secretion of this protein.

• Authors: E S Bochkareva, N M Lissin, A S Girshovich
• Journal: Nature (Nature) Vol. 336 Issue 6196 Pg. 254-7 (Nov 17 1988) ISSN: 0028-0836 [Print] England
• PMID: 2904124 (Publication Type: Journal Article)

Chemical References

• Affinity Labels
• Bacterial Proteins
• Chaperonin 60
• Cross-Linking Reagents
• Disulfides
• Enzyme Precursors
• Heat-Shock Proteins
• Adenosine Triphosphate
• Chloramphenicol O-Acetyltransferase
• beta-Lactamases
• Dithiothreitol

Topics

• Adenosine Triphosphate (pharmacology)
• Affinity Labels
• Bacterial Proteins (metabolism)
• Chaperonin 60
• Chloramphenicol O-Acetyltransferase (metabolism)
• Cross-Linking Reagents
• Disulfides (metabolism)
• Dithiothreitol (pharmacology)
• Enzyme Precursors (metabolism)
• Escherichia coli (metabolism)
• Heat-Shock Proteins (metabolism)
• Photochemistry
• Plasmids
• Protein Biosynthesis
• Protein Conformation
• Protein Processing, Post-Translational
• beta-Lactamases (metabolism)