Interactions of the DNA polymerase X from African Swine Fever Virus with the ssDNA. Properties of the total DNA-binding site and the strong DNA-binding subsite.
Biophys Chem
; 158(1): 26-37, 2011 Sep.
Article
in En
| MEDLINE
| ID: mdl-21601347
ABSTRACT
Interactions of the polymerase X from the African Swine Fever Virus with the ssDNA have been studied, using quantitative fluorescence titration and fluorescence resonance energy transfer techniques. The primary DNA-binding subsite of the enzyme, independent of the DNA conformation, is located on the C-terminal domain. Association of the bound DNA with the catalytic N-terminal domain finalizes the engagement of the total DNA-binding site of the enzyme and induces a large topological change in the structure of the bound ssDNA. The free energy of binding includes a conformational transition of the protein. Large positive enthalpy changes accompanying the ASFV pol X-ssDNA association indicate that conformational changes of the complex are induced by the engagement of the N-terminal domain. The enthalpy changes are offset by large entropy changes accompanying the DNA binding to the C-terminal domain and the total DNA-binding site, predominantly resulting from the release of water molecules.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
DNA, Single-Stranded
/
African Swine Fever Virus
/
DNA-Directed DNA Polymerase
Language:
En
Journal:
Biophys Chem
Year:
2011
Document type:
Article
Affiliation country:
United States