Biomaterial Database

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. 1992

P V Viitanen, and A A Gatenby, and G H Lorimer

Central Research and Development Department, E.I. Du Pont de Nemours & Co. Experimental Station, Wilmington, Delaware 19880-0402.

In vitro experiments employing the soluble proteins from Escherichia coli reveal that about half of them, in their unfolded or partially folded states, but not in their native states, can form stable binary complexes with chaperonin 60 (groEL). These complexes can be isolated by gel filtration chromatography and are efficiently discharged upon the addition of Mg.ATP. Binary complex formation is substantially reduced if chaperonin 60 is presaturated with Rubisco-I, the folding intermediate of Rubisco, but not with native Rubisco. Binary complex formation is also reduced if the transient species that interact with chaperonin 60 are permitted to progress to more stable states. This implies that the structural elements or motifs that are recognized by chaperonin 60 and that are responsible for binary complex formation are only present or accessible in the unfolded states of proteins or in certain intermediates along their respective folding pathways. Given the high-affinity binding that we have observed in the present study and the normal cellular abundance of chaperonin 60, we suspect that the folding of most proteins in E. coli does not occur in free solution spontaneously, but instead takes place while they are associated with molecular chaperones.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008715	Methionine	A sulfur-containing essential L-amino acid that is important in many body functions.	L-Methionine,Liquimeth,Methionine, L-Isomer,Pedameth,L-Isomer Methionine,Methionine, L Isomer
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006360	Heat-Shock Proteins	Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.	Stress Protein,Stress Proteins,Heat-Shock Protein,Heat Shock Protein,Heat Shock Proteins,Protein, Stress
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012247	Rhodospirillum rubrum	Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
D012273	Ribulose-Bisphosphate Carboxylase	A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.	Carboxydismutase,Ribulose Biphosphate Carboxylase-Oxygenase,Ribulose Diphosphate Carboxylase,Ribulosebiphosphate Carboxylase,Rubisco,1,5-Biphosphate Carboxylase-Oxygenase,Ribulose Biphosphate Carboxylase,Ribulose Bisphosphate Carboxylase,Ribulose-1,5-Biphosphate Carboxylase,Ribulose-1,5-Biphosphate Carboxylase-Oxygenase,Ribulose-1,5-Bisphosphate Carboxylase Small-Subunit,Ribulose-Bisphosphate Carboxylase Large Subunit,Ribulose-Bisphosphate Carboxylase Small Subunit,Rubisco Small Subunit,1,5 Biphosphate Carboxylase Oxygenase,Biphosphate Carboxylase-Oxygenase, Ribulose,Carboxylase Small-Subunit, Ribulose-1,5-Bisphosphate,Carboxylase, Ribulose Bisphosphate,Carboxylase, Ribulose Diphosphate,Carboxylase, Ribulose-1,5-Biphosphate,Carboxylase, Ribulose-Bisphosphate,Carboxylase, Ribulosebiphosphate,Carboxylase-Oxygenase, 1,5-Biphosphate,Carboxylase-Oxygenase, Ribulose Biphosphate,Carboxylase-Oxygenase, Ribulose-1,5-Biphosphate,Diphosphate Carboxylase, Ribulose,Ribulose 1,5 Biphosphate Carboxylase,Ribulose 1,5 Biphosphate Carboxylase Oxygenase,Ribulose 1,5 Bisphosphate Carboxylase Small Subunit,Ribulose Biphosphate Carboxylase Oxygenase,Ribulose Bisphosphate Carboxylase Large Subunit,Ribulose Bisphosphate Carboxylase Small Subunit,Small Subunit, Rubisco,Small-Subunit, Ribulose-1,5-Bisphosphate Carboxylase
D013462	Sulfur Radioisotopes	Unstable isotopes of sulfur that decay or disintegrate spontaneously emitting radiation. S 29-31, 35, 37, and 38 are radioactive sulfur isotopes.	Radioisotopes, Sulfur
D017510	Protein Folding	Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.	Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D018834	Chaperonin 60	A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.	Heat-Shock Proteins 60,hsp60 Family,GroEL Protein,GroEL Stress Protein,Heat-Shock Protein 60,hsp60 Protein,Heat Shock Protein 60,Heat Shock Proteins 60