Structure-function studies of DNA polymerase lambda.
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.
Garcia-Diaz
Miguel
M
Laboratory of Structural Biology and Laboratory of Molecular Genetics NIEHS, NIH, DHHS, Research Triangle Park, NC 27709, USA.
Bebenek
Katarzyna
K
Gao
Guanghua
G
Pedersen
Lars C
LC
London
Robert E
RE
Kunkel
Thomas A
TA
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
C423906:5'-deoxyribose phosphate lyase; C415367:DNA polymerase beta2; D019951:DNA Polymerase beta; D019761:Phosphorus-Oxygen Lyases