The iron-sulfur cluster is essential for DNA binding by human DNA polymerase ε.

ABSTRACT: DNA polymerase ε (Polε) is a key enzyme for DNA replication in eukaryotes. Recently it was shown that the catalytic domain of yeast Polε (Polε_CD) contains a [4Fe-4S] cluster located at the base of the processivity domain (P-domain) and coordinated by four conserved cysteines. In this work, we show that human Polε_CD (hPolε_CD) expressed in bacterial cells also contains an iron-sulfur cluster. In comparison, recombinant hPolε_CD produced in insect cells contains significantly lower level of iron. The iron content of purified hPolE_CD samples correlates with the level of DNA-binding molecules, which suggests an important role of the iron-sulfur cluster in hPolε interaction with DNA. Indeed, mutation of two conserved cysteines that coordinate

SUBMITTER: Lisova AE 

PROVIDER: S-EPMC9581978 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature