The human GINS complex binds to and specifically stimulates human DNA polymerase alpha-primase.

Abstract:

:The eukaryotic GINS complex has an essential role in the initiation and elongation phases of genome duplication. It is composed of four paralogous subunits--Sld5, Psf1, Psf2 and Psf3--which are ubiquitous and evolutionarily conserved in eukaryotic organisms. Here, we report the biochemical characterization of the human GINS complex (hGINS). The four hGINS subunits were coexpressed in Escherichia coli in a highly soluble form and purified as a complex. hGINS was shown to interact directly with the heterodimeric human DNA primase, by using either surface plasmon resonance measurements or by immunoprecipitation experiments carried out with anti-hGINS antibodies. The DNA polymerase alpha-primase synthetic activity was specifically stimulated by hGINS on various primed DNA templates. The significance of these findings is discussed in view of the molecular dynamics at the human replication fork.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

De Falco M,Ferrari E,De Felice M,Rossi M,Hübscher U,Pisani FM

doi

10.1038/sj.embor.7400870

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

99-103

issue

1

eissn

1469-221X

issn

1469-3178

pii

7400870

journal_volume

8

pub_type

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