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

Bacteriophage T4 helicase loader protein gp59 functions as gatekeeper in origin-dependent replication in vivo.

The Journal of biological chemistry - 3 Jun 2005

Dudas Kathleen C, Kreuzer Kenneth N

Abstract excerpt

Bacteriophage T4 initiates origin-dependent replication via an R-loop mechanism in vivo. During in vitro reactions, the phage-encoded gp59 stimulates loading of the replicative helicase, gp41, onto branched intermediates, including origin R-loops. However, although gp59 is essential for recombination-dependent replication from D-loops, it does not appear to be required for origin-dependent replication in vivo. In...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophage T4
Share to DNA, Single-Stranded
Share to Electrophoresis, Agar Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Gel, Two-Dimensional

Share to Replication Origin

Share to Viral Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 15781450
DOI: 10.1074/jbc.M502351200
PMCID: PMC1361368

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

Bacteriophage T4 helicase loader protein gp59 functions as gatekeeper in origin-dependent replication in vivo.PMID 15781450Read ↗

Origin activation requires both replicative and accessory helicases during T4 infection.Semantic proximity Read ↗

Dual functions of single-stranded DNA-binding protein in helicase loading at the bacteriophage T4 DNA replication fork.Semantic proximity Read ↗

The helicase domain of phage P4 alpha protein overlaps the specific DNA binding domain.Semantic proximity Read ↗

Divergence of a DNA replication gene cluster in the T4-related bacteriophage RB69.Semantic proximity Read ↗

Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis.Semantic proximity Read ↗

Mutations of bacteriophage T4 59 helicase loader defective in binding fork DNA and in interactions with T4 32 single-stranded DNA-binding protein.Semantic proximity Read ↗

UvsW protein regulates bacteriophage T4 origin-dependent replication by unwinding R-loops.Semantic proximity Read ↗

Regression supports two mechanisms of fork processing in phage T4.Semantic proximity Read ↗

Multiple origins of replication contribute to a discontinuous pattern of DNA synthesis across the T4 genome during infection.Semantic proximity Read ↗

The mycobacteriophage D29 gene 65 encodes an early-expressed protein that functions as a structure-specific nuclease.Semantic proximity Read ↗

Genome replication and progeny virion production of herpes simplex virus type 1 mutants with temperature-sensitive lesions in the origin-binding protein.Semantic proximity Read ↗

The vaccinia virus-encoded uracil DNA glycosylase has an essential role in viral DNA replication.Semantic proximity Read ↗

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