Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymerase

29 Jun 2021

Abstract excerpt

PrimPol is a human DNA polymerase-primase that localizes to mitochondria and nucleus and bypasses the major oxidative lesion 7,8-dihydro-8-oxoguanine (oxoG) via translesion synthesis, in mostly error-free manner. We present structures of PrimPol insertion complexes with a DNA template-primer and correct dCTP or erroneous dATP opposite the lesion, as well as extension complexes with C or A as a 3'-terminal primer...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CRISPR and Genetic Engineering
Share to Cytomegalovirus and herpesvirus research
Share to DNA Repair Mechanisms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34188055
DOI: 10.1038/s41467-021-24317-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymerasePMID 34188055Read ↗

Translesion activity of PrimPol on DNA with cisplatin and DNA–protein cross-linksSemantic proximity Read ↗

Mutagenesis mechanism of the major oxidative adenine lesion 7,8-dihydro-8-oxoadenine.Semantic proximity Read ↗

DNA polymerase α-primase can function as a translesion DNA polymeraseSemantic proximity Read ↗

PrimPol is required for the maintenance of efficient nuclear and mitochondrial DNA replication in human cellsSemantic proximity Read ↗

PrimPol is required for the maintenance of efficient nuclear and mitochondrial DNA replication in human cellsSemantic proximity Read ↗

PrimPol variant V102A with altered primase and polymerase activitiesSemantic proximity Read ↗

Mitochondrial DNA replication: a PrimPol perspective.Semantic proximity Read ↗

Unexpected non-Hoogsteen-based mutagenicity mechanism of FaPy-DNA lesions.Semantic proximity Read ↗

The steric gate of DNA polymerase ι regulates ribonucleotide incorporation and deoxyribonucleotide fidelity.Semantic proximity Read ↗

S phase R-loop formation is restricted by PrimPol-mediated reprimingSemantic proximity Read ↗

Regulation of oxidative DNA damage repair: the adenine:8-oxo-guanine problem.Semantic proximity Read ↗

Engineering human PrimPol into an efficient RNA-dependent-DNA primase/polymerase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.