Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 8 (2), 417-26

Structure of the Catalytic Core of S. Cerevisiae DNA Polymerase Eta: Implications for Translesion DNA Synthesis

Affiliations

Structure of the Catalytic Core of S. Cerevisiae DNA Polymerase Eta: Implications for Translesion DNA Synthesis

J Trincao et al. Mol Cell.

Abstract

DNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25A resolution. The structure reveals a novel polydactyl right hand-shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer.

Similar articles

See all similar articles

Cited by 114 PubMed Central articles

See all "Cited by" articles

Publication types

MeSH terms

Associated data

LinkOut - more resources

Feedback