Reversible dissociation and unfolding of the dimeric protein thymidylate synthase.


Abstract

Conditions for in vitro unfolding and refolding of dimeric thymidylate synthase from Lactobacillus casei were found. Ultraviolet difference and circular dichroism spectra showed that the enzyme was completely unfolded at concentrations of urea over 5.5 M. As measured by restoration of enzyme activity, refolding was accomplished when 0.5 M potassium chloride was included in the refolding mixture. Recombination of subunits from catalytically inactive mutant homodimers to form an active hybrid dimer was achieved under these unfolding-refolding conditions, demonstrating a monomer to dimer association step. Study holds ProTherm entries: 10382 Extra Details: additive : EDTA(0.1 mM), dimerization; folding; oligomerization; thymidylate synthase

Submission Details

ID: fw7pNpXU3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Perry KM;Pookanjanatavip M;Zhao J;Santi DV;Stroud RM,Protein Sci. (1992) Reversible dissociation and unfolding of the dimeric protein thymidylate synthase. PMID:1304920
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