Shared active site architecture between the large subunit of eukaryotic primase and DNA photolyase.

ABSTRACT:

Background

DNA synthesis during replication relies on RNA primers synthesised by the primase, a specialised DNA-dependent RNA polymerase that can initiate nucleic acid synthesis de novo. In archaeal and eukaryotic organisms, the primase is a heterodimeric enzyme resulting from the constitutive association of a small (PriS) and large (PriL) subunit. The ability of the primase to initiate synthesis of an RNA primer depends on a conserved Fe-S domain at the C-terminus of PriL (PriL-CTD). However, the critical role of the PriL-CTD in the catalytic mechanism of initiation is not understood.

Methodology/principal findings

Here we report the crystal structure of the yeast PriL-CTD at 1.55 A resolution. The structure reveals that the PriL-CTD folds in two largely independent alpha-h

SUBMITTER: Sauguet L 

PROVIDER: S-EPMC2852410 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature