Discover Community Create You

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

A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates.

Nature - 12 Jan 2006

Jarosz Daniel F, Godoy Veronica G, Delaney James C, Essigmann John M, Walker Graham C

Abstract excerpt

Translesion synthesis (TLS) by Y-family DNA polymerases is a chief mechanism of DNA damage tolerance. Such TLS can be accurate or error-prone, as it is for bypass of a cyclobutane pyrimidine dimer by DNA polymerase eta (XP-V or Rad30) or bypass of a (6-4) TT photoproduct by DNA polymerase V (UmuD'2C), respectively. Although DinB is the only Y-family DNA polymerase conserved among all domains of life, the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Base Pair Mismatch
Share to Catalysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Deoxyguanosine

Share to DNA Adducts

Share to DNA-Directed DNA Polymerase

Share to Mutagens

Share to Templates, Genetic

Source

Identifiers

PMID: 16407906
DOI: 10.1038/nature04318

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates.PMID 16407906Read ↗

A DinB variant reveals diverse physiological consequences of incomplete TLS extension by a Y-family DNA polymeraseSemantic proximity Read ↗

An active site aromatic triad in Escherichia coli DNA Pol IV coordinates cell survival and mutagenesis in different DNA damaging agents.Semantic proximity Read ↗

UmuD and RecA directly modulate the mutagenic potential of the Y family DNA polymerase DinB.Semantic proximity Read ↗

Human polymerase kappa uses a template-slippage deletion mechanism, but can realign the slipped strands to favour base substitution mutations over deletions.Semantic proximity Read ↗

Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors.Semantic proximity Read ↗

The steric gate amino acid tyrosine 112 is required for efficient mismatched-primer extension by human DNA polymerase kappa.Semantic proximity Read ↗

Human <i>DINB1</i> -encoded DNA polymerase κ is a promiscuous extender of mispaired primer terminiSemantic proximity Read ↗

A multilayered repair system protects the mycobacterial chromosome from endogenous and antibiotic-induced oxidative damage.Semantic proximity Read ↗

Translesion DNA synthesis: little fingers teach tolerance.Semantic proximity Read ↗

Structure and mechanism of error-free replication past the major benzo[a]pyrene adduct by human DNA polymerase κSemantic proximity Read ↗

Structural and functional elucidation of the mechanism promoting error-prone synthesis by human DNA polymerase kappa opposite the 7,8-dihydro-8-oxo-2'-deoxyguanosine adduct.Semantic proximity Read ↗

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

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