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

Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial non-homologous end-joining protein, DNA ligase D.

The Journal of biological chemistry - 15 Jul 2005

Zhu Hui, Shuman Stewart

Abstract excerpt

Pseudomonas aeruginosa DNA ligase D (PaeLigD) exemplifies a family of bacterial DNA end-joining proteins that consist of a ligase domain fused to a polymerase domain and a putative nuclease module. The LigD polymerase preferentially adds single ribonucleotides at blunt DNA ends and, as we show here, is also capable of adding up to 4 ribonucleotides to a DNA primer-template. We report that PaeLigD has an intrinsic...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Aspartic Acid
Share to Centrifugation, Density Gradient

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Ligase ATP

Share to DNA Ligases

Share to Glycerol

Share to Phosphoric Monoester Hydrolases

Share to Ribonucleases

Source

Identifiers

PMID: 15897197
DOI: 10.1074/jbc.M504002200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial non-homologous end-joining protein, DNA ligase D.PMID 15897197Read ↗

Substrate specificity and structure-function analysis of the 3'-phosphoesterase component of the bacterial NHEJ protein, DNA ligase D.Semantic proximity Read ↗

Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D.Semantic proximity Read ↗

Gap filling activities of Pseudomonas DNA ligase D (LigD) polymerase and functional interactions of LigD with the DNA end-binding Ku protein.Semantic proximity Read ↗

DNA Ligases: Progress and ProspectsSemantic proximity Read ↗

An RNA ligase from Deinococcus radiodurans.Semantic proximity Read ↗

Nucleotide misincorporation, 3'-mismatch extension, and responses to abasic sites and DNA adducts by the polymerase component of bacterial DNA ligase D.Semantic proximity Read ↗

Structural Determinants Responsible for the Preferential Insertion of Ribonucleotides by Bacterial NHEJ PolDom.Semantic proximity Read ↗

Deinococcus radiodurans HD-Pnk, a Nucleic Acid End-Healing Enzyme, Abets Resistance to Killing by Ionizing Radiation and Mitomycin C.Semantic proximity Read ↗

Structure and mechanism of the 2',3' phosphatase component of the bacterial Pnkp-Hen1 RNA repair system.Semantic proximity Read ↗

Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine.Semantic proximity Read ↗

Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D.Semantic proximity Read ↗

Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+.Semantic proximity Read ↗

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