Prevalence of temperature-dependent heat capacity changes in protein-DNA interactions.
A large, negative DeltaCp of DNA binding is a thermodynamic property of the majority of sequence-specific DNA-protein interactions, and a common, but not universal property of non-sequence-specific DNA binding. In a recent study of the binding of Taq polymerase to DNA, we showed that both the full-length polymerase and its "Klentaq" large fragment bind to primed-template DNA with significant negative heat capacities. Herein, we have extended this analysis by analyzing this data for temperature-variable heat capacity effects (DeltaDeltaCp), and have similarly analyzed an additional 47 protein-DNA binding pairs from the scientific literature. Over half of the systems examined can be easily fit to a function that includes a DeltaDeltaCp parameter. Of these, 90% display negative DeltaDeltaCp values, with the result that the DeltaCp of DNA binding will become more negative with rising temperature. The results of this collective analysis have potentially significant consequences for current quantitative theories relating DeltaCp values to changes in accessible surface area, which rely on the assumption of temperature invariance of the DeltaCp of binding. Solution structural data for Klentaq polymerase demonstrate that the observed heat capacity effects are not the result of a coupled folding event.
Liu
Chin-Chi
CC
Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana, USA.
Richard
Allison J
AJ
Datta
Kausiki
K
LiCata
Vince J
VJ
D003198:Computer Simulation; D004247:DNA / Q000737:chemistry* / Q000648:ultrastructure*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D004735:Energy Transfer; D006358:Hot Temperature; D008956:Models, Chemical; D008958:Models, Molecular; D009691:Nucleic Acid Denaturation; D011489:Protein Denaturation; D013696:Temperature
D004268:DNA-Binding Proteins; D004247:DNA