Approaching the crystal structure of the polymerase γ catalytic complex
MetadataShow full item record
In this thesis, a 4.7Å crystal structure of the human mitochondria DNA polymerase γ catalytic complex is reported. Though the DNA substrate-binding site is not identifiable in the structure, two conformational changes in the enzyme architecture are described: 1) rotation of the distal monomer of the accessory subunit towards the catalytic subunit, and 2) shift of the thumb motif of the polymerase domain towards the active site. Both conformational changes suggest a structure of Pol γ in the DNA-bound state and in its active site “closed” conformation.
Showing items related by title, author, creator and subject.
Studies of the metal binding properties and DNA recognition mode of the unusual zinc fingers in poly(ADP-ribose) Polymerase-1 and the investigation of its interaction with apoptosis inducing factor (AIF) Zhou, Ying, 1977- (2009-08)Poly(ADP-ribosyl)ation, a covalent modification of proteins catalyzed by poly(ADP-ribose) polymerases (PARPs), plays a crucial role in regulating DNA repair, DNA replication, and cell death. Poly(ADP-ribose) Polymerase-1 ...
Kinetics and specificity of human mitochondrial DNA polymerase gamma and HIV-1 reverse transcriptase Ziehr, Jessica Lea (2014-08)The human mitochondrial DNA (mtDNA) genome must be faithfully maintained by the mitochondrial DNA replication machinery. Deficiencies in mtDNA maintenance result in the accumulation of mutations and deletions, which have ...
Hawkins, Michael Andrew; 0000-0001-8850-5086 (2019-01-31)Cellular life is precarious. Dangers abound for a cell’s DNA, from both external and internal factors, and maintaining genomic integrity is crucial for cell survival. Oxidative damage, from reactive oxygen/nitrogen species, ...