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Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster

DOI: 10.1038/s41467-017-01707-w DOI Help

Authors: Sandro Holzer (University of Cambridge) , Jiangyu Yan (Indiana University) , Mairi L. Kilkenny (University of Cambridge) , Stephen D. Bell (Indiana University) , Luca Pellegrini (University of Cambridge, U.K.)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: December 2017

Open Access Open Access

Abstract: DNA replication depends on primase, the specialised polymerase responsible for synthesis of the RNA primers that are elongated by the replicative DNA polymerases. In eukaryotic and archaeal replication, primase is a heterodimer of two subunits, PriS and PriL. Recently, a third primase subunit named PriX was identified in the archaeon Sulfolobus solfataricus. PriX is essential for primer synthesis and is structurally related to the Fe–S cluster domain of eukaryotic PriL. Here we show that PriX contains a nucleotide-binding site required for primer synthesis, and demonstrate equivalence of nucleotide-binding residues in PriX with eukaryotic PriL residues that are known to be important for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe–S cluster domain retains wild-type levels of primer synthesis. Our evidence shows that PriX has replaced PriL as the subunit that endows primase with the unique ability to initiate nucleic acid synthesis. Importantly, our findings reveal that the Fe–S cluster is not required for primer synthesis.

Journal Keywords: DNA synthesis; Enzyme mechanisms; X-ray crystallography

Diamond Keywords: Enzyme; Archaea

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

Added On: 05/01/2018 14:56


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)