Event Title
Location
University of Richmond, Richmond, Virginia
Document Type
Poster (UR Campus Access Only)
Description
All organisms replicate DNA to be used during cell division and passed on to offspring. In order for this process to occur, DNA polymerase I must form base pairs between complementary nucleotides. Deprotonation of the primer 3’-OH strand readies the DNA for forming a covalent bond with the next nucleotide. Histidine 829 is a potential proton acceptor, seeing as its imidazole side chain has a pKa≈6. Here, we report X-ray crystal structures of H829A, H829F and H829G. Mutations to histidine 829 led to changes in the orientation of nearby residues. Kinetics studies would show whether these mutations lead to changes in the activity of DNA polymerase I.
Effects of mutations of highly conserved active site histidine on DNA polymerase I structure and activity
University of Richmond, Richmond, Virginia
All organisms replicate DNA to be used during cell division and passed on to offspring. In order for this process to occur, DNA polymerase I must form base pairs between complementary nucleotides. Deprotonation of the primer 3’-OH strand readies the DNA for forming a covalent bond with the next nucleotide. Histidine 829 is a potential proton acceptor, seeing as its imidazole side chain has a pKa≈6. Here, we report X-ray crystal structures of H829A, H829F and H829G. Mutations to histidine 829 led to changes in the orientation of nearby residues. Kinetics studies would show whether these mutations lead to changes in the activity of DNA polymerase I.
Comments
Department: Biology
Faculty Mentor: Dr. Eugene Wu