title: Structure-function studies of DNA polymerase lambda.
abstract: DNA polymerase lambda is a member of the X family of polymerases that is implicated in non-homologous end-joining of double-strand breaks in DNA and in base excision repair of DNA damage. To better understand the roles of DNA polymerase lambda in these repair pathways, here we review its structure and biochemical properties, with emphasis on its gap-filling polymerization activity, its dRP lyase activity and its unusual DNA synthetic (in)fidelity.
authors.affiliation: Laboratory of Structural Biology and Laboratory of Molecular Genetics NIEHS, NIH, DHHS, Research Triangle Park, NC 27709, USA.
authors.forename: Miguel
authors.initials: M
authors.lastname: Garcia-Diaz
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Bebenek
authors.forename: Guanghua
authors.initials: G
authors.lastname: Gao
authors.forename: Lars C
authors.initials: LC
authors.lastname: Pedersen
authors.forename: Robert E
authors.initials: RE
authors.lastname: London
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Kunkel
mesh_terms: D019951:DNA Polymerase beta / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D006801:Humans; D009690:Nucleic Acid Conformation; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
chemical_list: C423906:5'-deoxyribose phosphate lyase; C415367:DNA polymerase beta2; D019951:DNA Polymerase beta; D019761:Phosphorus-Oxygen Lyases