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

Identification of the Dimer Exchange Interface of the Bacterial DNA Damage Response Protein UmuD.

Biochemistry - 12 Sept 2017

Murison David A, Timson Rebecca C, Koleva Bilyana N, Ordazzo Michael, Beuning Penny J

Abstract excerpt

The Escherichia coli SOS response, an induced DNA damage response pathway, confers survival on bacterial cells by providing accurate repair mechanisms as well as the potentially mutagenic pathway translesion synthesis (TLS). The umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response. Full-length UmuD is expressed as a homodimer of...

Read the complete abstract on PubMed

Topics

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

Share to DNA Damage
Share to Escherichia coli Proteins
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Plasmids

Share to Protein Conformation

Share to Protein Subunits

Share to Serine Endopeptidases

Share to SOS Response, Genetics

Source

Identifiers

PMID: 28806503
DOI: 10.1021/acs.biochem.7b00560

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of the Dimer Exchange Interface of the Bacterial DNA Damage Response Protein UmuD.PMID 28806503Read ↗

Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage.Semantic proximity Read ↗

The UmuD' protein filament and its potential role in damage induced mutagenesis.Semantic proximity Read ↗

Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.Semantic proximity Read ↗

Regulation of UmuD cleavage: role of the amino-terminal tail.Semantic proximity Read ↗

Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis.Semantic proximity Read ↗

A structural model for the damage-sensing complex in bacterial nucleotide excision repair.Semantic proximity Read ↗

Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity.Semantic proximity Read ↗

A non-cleavable UmuD variant that acts as a UmuD' mimic.Semantic proximity Read ↗

Mutations affecting the ability of the Escherichia coli UmuD' protein to participate in SOS mutagenesis.Semantic proximity Read ↗

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

5'-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase.Semantic proximity Read ↗

Mobile element integration reveals a chromosome dimer resolution system in LegionellalesSemantic proximity Read ↗

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