Biochemical characterization and mutational analysis of a mismatch glycosylase from the hyperthermophilic euryarchaeon Thermococcus barophilus Ch5

Thermococcus kodakarensis TK0353 is a novel AP lyase with a new fold

“…Previous work on DNA repair enzymes from Thermococcales reveals a variety of bifunctional glycosylases that remove damaged nucleobases and cleave the resulting AP sites. These enzymes, including AGOG ( 33 ), Tba uracil DNA glycosylase (UDG247) ( 34 ), endonuclease III ( 35 ) and Tb-Mig ( 36 ), encode both a primary repair glycosylase activity that first recognizes and removes damaged (or mismatched) nucleobases producing AP sites that are then cleaved by the AP lyase activity, with both activities on the same polypeptide. For example, the AGOG glycosylase activity cleaves 8-oxoG, and then the associated AP lyase activity cleaves the remaining AP site, leaving a one nucleotide gap with 3′ and 5′ phosphates ( 33 ).…”