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 Repjournal_title
EMBO reportsauthors
De Falco M,Ferrari E,De Felice M,Rossi M,Hübscher U,Pisani FMdoi
10.1038/sj.embor.7400870subject
Has Abstractpub_date
2007-01-01 00:00:00pages
99-103issue
1eissn
1469-221Xissn
1469-3178pii
7400870journal_volume
8pub_type
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