Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase beta 2 subunits. 1996

T Planchenault, and A Navon, and A J Schulze, and M E Goldberg
Unité de Biochimie Cellulaire (CNRS URA 1129), Institut Pasteur, Paris, France.

Local structures formed in early intermediates are thought to play a key role in orientating the protein folding pathway. Here, we test whether non-native interactions formed by eight N-terminal residues in early folding intermediates of tryptophan synthase beta chains [Navon, A., Schulze, A. J., Guillou, Y., Zylinksii, C. A., Baleux, F., Expert-Bezançon, N., Friguet, B., Djavadi-Ohaniance, L. & Goldberg, M. E. (1995) J. Biol. Chem. 270, 4255-4261] influence the folding kinetics. The kinetics of in vitro renaturation of wild-type beta chains and truncated beta chains lacking residues 2-9 were compared. Each step analyzed (molten globule formation, tryptophan shielding, closing up of distant residues, and complete renaturation) occurred with similar kinetics in the normal and truncated proteins. Thus, non-native interactions formed early during the folding of beta chains seem to influence neither the rate and efficiency of the complete renaturation, nor the kinetics of the early folding steps, which suggests that such non-native early intermediates are poorly stable and highly dynamic. This observation is consistent with the current view that productive folding should avoid the formation of stable intermediates.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
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
D005456 Fluorescent Dyes Chemicals that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags. Flourescent Agent,Fluorescent Dye,Fluorescent Probe,Fluorescent Probes,Fluorochrome,Fluorochromes,Fluorogenic Substrates,Fluorescence Agents,Fluorescent Agents,Fluorogenic Substrate,Agents, Fluorescence,Agents, Fluorescent,Dyes, Fluorescent,Probes, Fluorescent,Substrates, Fluorogenic
D000817 Anilino Naphthalenesulfonates A class of organic compounds which contain an anilino (phenylamino) group linked to a salt or ester of naphthalenesulfonic acid. They are frequently used as fluorescent dyes and sulfhydryl reagents. Naphthalenesulfonates, Anilino
D012545 Schiff Bases Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed) Schiff Base,Base, Schiff,Bases, Schiff
D013050 Spectrometry, Fluorescence Measurement of the intensity and quality of fluorescence. Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence
D014364 Tryptophan An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals. Ardeydorm,Ardeytropin,L-Tryptophan,L-Tryptophan-ratiopharm,Levotryptophan,Lyphan,Naturruhe,Optimax,PMS-Tryptophan,Trofan,Tryptacin,Tryptan,Tryptophan Metabolism Alterations,ratio-Tryptophan,L Tryptophan,L Tryptophan ratiopharm,PMS Tryptophan,ratio Tryptophan
D014367 Tryptophan Synthase An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and water and of indoleglycerol phosphate into indole and glyceraldehyde phosphate. (From Enzyme Nomenclature, 1992) EC 4.2.1.20. Tryptophan Synthetase,Synthase, Tryptophan,Synthetase, Tryptophan
D017384 Sequence Deletion Deletion of sequences of nucleic acids from the genetic material of an individual. Deletion Mutation,Deletion Mutations,Deletion, Sequence,Deletions, Sequence,Mutation, Deletion,Mutations, Deletion,Sequence Deletions

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