Kinetics of the unfolding-folding transition of Bacillus subtilis levansucrase precursor.
The reversible folding-unfolding transition of mature and precursor forms of Bacillus subtilis levansucrase were compared under physiological conditions of pH and temperature. The time constant of the folding reaction was not modified by the presence of the signal sequence and the precursor in the native form was slightly more resistant to the denaturing action of urea. However, the folding pathway could be different for each protein since a domain of the mature levansucrase underwent an independent transition which is not observed during the renaturation process of prelevansucrase.
Scotti
P A
PA
Institut Jacques Monod, CNRS, Université Paris VII Laboratoire Génétique et Membranes, France.
Chambert
R
R
Petit-Glatron
M F
MF
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry; D006602:Hexosyltransferases / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation; D017510:Protein Folding; D013381:Subtilisins / Q000494:pharmacology; D013696:Temperature
D001426:Bacterial Proteins; D006602:Hexosyltransferases; C021513:levansucrase; D013381:Subtilisins