Project description: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.

| S-EPMC1796748 | biostudies-literature

Movies for human polymerase alpha-primase in DNA elongation states

Project description: Not available

| EMPIAR-11361 | biostudies-other

Cryo-EM structure of human DNA polymerase alpha-primase at handover

Project description: Not available

| EMPIAR-11721 | biostudies-other

Cryo-EM structure of human DNA polymerase alpha-primase at initiation

Project description: Not available

| EMPIAR-11676 | biostudies-other

Cryo-EM structure of human DNA polymerase alpha-primase in pre-initiation stage 1

Project description: Not available

| EMPIAR-11643 | biostudies-other

Structure and mechanism of human PrimPol, a DNA polymerase with primase activity.

Project description:PrimPol is a novel human enzyme that contains both DNA primase and DNA polymerase activities. We present the first structure of human PrimPol in ternary complex with a DNA template-primer and an incoming deoxynucleoside triphosphate (dNTP). The ability of PrimPol to function as a DNA primase stems from a simple but remarkable feature-almost complete lack of contacts to the DNA primer strand. This, in turn, allows two dNTPs to bind initiation and elongation sites on the enzyme for the formation of the first dinucleotide. PrimPol shows the ability to synthesize DNA opposite ultraviolet (UV) lesions; however, unexpectedly, the active-site cleft of the enzyme is constrained, which precludes the bypass of UV-induced DNA lesions by conventional translesion synthesis. Together, the structure addresses long-standing questions about how DNA primases actually initiate synthesis and how primase and polymerase activities combine in a single enzyme to carry out DNA synthesis.

| S-EPMC5088642 | biostudies-literature

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