PMID:14766221
| Citation |
Sarfo, KJ, Winstone, TL, Papish, AL, Howell, JM, Kadir, H, Vogel, HJ and Turner, RJ (2004) Folding forms of Escherichia coli DmsD, a twin-arginine leader binding protein. Biochem. Biophys. Res. Commun. 315:397-403 |
|---|---|
| Abstract |
Escherichia coli DmsD interacts with the twin-arginine leader sequence of the catalytic sub-unit (DmsA) of DMSO reductase. DmsD was purified as a mixture of a number of different folding forms including: dimer (A); monomer (B); a minor thiol oxidized form; a heterogeneously folded or multi-conformational monomer form which displayed a ladder of bands on native-PAGE (D); and proteolytically degraded and aggregated forms. Polyacrylamide gel electrophoresis (PAGE), under denaturing and non-denaturing conditions, was used to examine the folding and stability of DmsD. Additionally, the biophysical methods of dynamic light scattering, circular dichroism, fluorescence, and mass spectroscopy were also used. Form D could be converted to form B by treatment with 4M urea, which is the concentration at which form B begins to denature. Forms A/B could be converted to D by incubation at pH 5.0. Forms A/B and D all had twin-arginine leader binding activity. |
| Links |
PubMed Online version:10.1016/j.bbrc.2004.01.070 |
| Keywords |
Arginine/chemistry; Blotting, Western; Catalytic Domain; Circular Dichroism; Dimerization; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Light; Mass Spectrometry; Membrane Transport Proteins/chemistry; Oxidoreductases/chemistry; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Sulfhydryl Compounds; Urea/pharmacology |
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