Dissociation constants and thermal stability of complexes of Bacillus intermedius RNase and the protein inhibitor of Bacillus amyloliquefaciens RNase.
Binase, the extracellular ribonuclease of Bacillus intermedius, is inhibited by barstar, the natural protein inhibitor of the homologous RNase, barnase, of B. intermedius. The dissociation constants of the binase complexes with barstar and its double Cys40,82Ala mutant are about 10(-12) M, only 5 to 43 times higher than those of the barnase-barstar complex. As with barnase, the denaturation temperature of binase is raised dramatically in the complex. Calorimetric studies of the formation and stability of the binase-barstar complex show that the binase reaction with barstar is qualitatively similar to that of barnase but some significant quantitative differences are reported.
Yakovlev
G I
GI
Engelhardt Institute of Molecular Biology, Acad. Sci. Russia, Moscow.
Moiseyev
G P
GP
Protasevich
I I
II
Ranjbar
B
B
Bocharov
A L
AL
Kirpichnikov
M P
MP
Gilli
R M
RM
Briand
C M
CM
Hartley
R W
RW
Makarov
A A
AA
D001407:Bacillus / Q000378:metabolism*; D001426:Bacterial Proteins / Q000494:pharmacology*; D002151:Calorimetry; D004722:Endoribonucleases / Q000037:antagonists & inhibitors*; D007700:Kinetics; D011485:Protein Binding; D011489:Protein Denaturation; D013045:Species Specificity; D013696:Temperature
D001426:Bacterial Proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D004722:Endoribonucleases; C022543:ribonuclease T(2)