Lee R Wiederhold

TL;DR: It is shown that in mammalian cells, removal of the 3' phosphate is dependent on polynucleotide kinase (PNK), and not APE, and that NEIL1/PNK could also repair the products of other DNA glycosylases, suggesting a broad role for this APE-independent BER pathway in mammals.

TL;DR: The key to understand the complete BER process is to elucidate how multiple proteins interact with one another in a coordinated process under specific physiological conditions.

TL;DR: The mtAPE-sized product could be generated by incubating 35S-labeled APE1 with crude mitochondrial extract, but not with cytosolic or nuclear extract, suggesting that cleavage of APE 1 by a specific mitochondria-associated N-terminal peptidase is a prerequisite for mitochondrial import.

TL;DR: It is shown that theNEIL2-initiated repair of 5-hydroxyuracil (5-OHU) similarly requires PNK, and stable interaction between NEIL2 and other BER proteins DNA polymerase beta (Pol beta), DNA ligase IIIalpha (Lig IIIalpha) and XRCC1 is observed.

TL;DR: NEIL1, a DNA glycosylase/AP lyase specific for many oxidized bases but with weak 8-oxoG excision activity, stimulates turnover of OGG1 in a fashion similar to that of APE1 and carries out betadelta-elimination at the AP site.