Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person At HHV8 ori-Lyt, the viral DNA polymerase ORF9 catalyses tem...
| Class:Id | Summation:9991203 |
|---|---|
| _displayName | At HHV8 ori-Lyt, the viral DNA polymerase ORF9 catalyses tem... |
| _timestamp | 2026-06-04 16:39:14 |
| created | [InstanceEdit:9991213] Stephan, Ralf, 2026-06-04 |
| text | At HHV8 ori-Lyt, the viral DNA polymerase ORF9 catalyses template-directed addition of dNTPs onto the 3′ end of RNA-primed nascent strands, releasing pyrophosphate (PPi), while the processivity factor ORF59 tethers ORF9 to the DNA to enable synthesis of long product strands; ORF9 on its own incorporates only a few nucleotides before dissociating (Chan and Chandran, 2000). Together with ORF59 it extends viral DNA in a rolling-circle mode, generating long head-to-tail concatemers that are subsequently cleaved into unit-length genomes for packaging (Hollingworth et al. 2017). This process is supported primarily by the demonstrated polymerase holoenzyme activity and by the observation that newly synthesised concatemeric viral DNA accumulates in these compartments free of cellular histones (Hollingworth et al. 2017).Both ORF9 and ORF59 were shown to be essential trans-acting factors for ori-Lyt-dependent replication in cotransfection-replication assays in which omission of either gene abolished DpnI-resistant plasmid amplification (AuCoin et al. 2004). Purified full-length ORF59 further assembles into hexameric/dodecameric ring structures with a central pore wide enough to encircle duplex DNA and binds preferentially to discrete ori-Lyt sites, consistent with a sliding-clamp mode of action during elongation (Travis et al. 2025). |
| (summation) | [BlackBoxEvent:9991180] Primer extension and rolling-circle DNA replication [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by At HHV8 ori-Lyt, the viral DNA polymerase ORF9 catalyses tem... (9991203)
