Stabilization of T4 polynucleotide kinase by macromolecular crowding.
T4 polynucleotide kinase rapidly loses activity during its reaction on duplex DNA termini. Addition of high concentrations of nonspecific polymers reverses or prevents this inactivation. In contrast, additions of related materials of lower molecular weight are relatively ineffective in stabilizing the kinase. Such a pattern suggests that the stabilizing effects of polymers on kinase activity are due to macromolecular crowding. An effect of crowding on the known tendency of the kinase to undergo oligomerization reactions is consistent with our observations.
D004247:DNA / Q000378:metabolism; D004789:Enzyme Activation; D007700:Kinetics; D010770:Phosphotransferases / Q000378:metabolism*; D011108:Polymers; D011116:Polynucleotide 5'-Hydroxyl-Kinase / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013604:T-Phages / Q000201:enzymology; D013696:Temperature; D013816:Thermodynamics
D011108:Polymers; D004247:DNA; D010770:Phosphotransferases; D011116:Polynucleotide 5'-Hydroxyl-Kinase