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

Genetic analysis of the interaction between bacteriophage T7 DNA polymerase and Escherichia coli thioredoxin.

Proceedings of the National Academy of Sciences of the United States of America - 15 Oct 1992

Himawan J S, Richardson C C

Abstract excerpt

Gene 5 protein of bacteriophage T7 is a nonprocessive DNA polymerase. During infection of Escherichia coli, T7 annexes the host protein thioredoxin for use as a processivity factor for T7 DNA polymerase. We describe here a genetic method to investigate the interaction between T7 gene 5 protein and E. coli thioredoxin. The strategy is to use thioredoxin mutants that are unable to support the growth of wild-type T7...

Read the complete abstract on PubMed

Topics

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

Share to DNA Replication
Share to Escherichia coli

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

Share to Genetic Complementation Test

Share to Macromolecular Substances

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Structure-Activity Relationship

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 1409697
DOI: 10.1073/pnas.89.20.9774
PMCID: PMC50215

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

Genetic analysis of the interaction between bacteriophage T7 DNA polymerase and Escherichia coli thioredoxin.PMID 1409697Read ↗

Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase.Semantic proximity Read ↗

Mutation of Phe102 to Ser in the carboxyl terminal helix of Escherichia coli thioredoxin affects the stability and processivity of T7 DNA polymerase.Semantic proximity Read ↗

Real-time kinetics of the interaction between the two subunits, Escherichia coli thioredoxin and gene 5 protein of phage T7 DNA polymerase.Semantic proximity Read ↗

C-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA.Semantic proximity Read ↗

Gene 1.7 of bacteriophage T7 confers sensitivity of phage growth to dideoxythymidine.Semantic proximity Read ↗

Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant.Semantic proximity Read ↗

A single-stranded DNA-binding protein of bacteriophage T7 defective in DNA annealing.Semantic proximity Read ↗

Reduction of mutant phage T4 glutaredoxins by Escherichia coli thioredoxin reductase.Semantic proximity Read ↗

Control of bacteriophage T4 tail lysozyme activity during the infection process.Semantic proximity Read ↗

Mutational and functional analysis of a segment of the sigma family bacteriophage T4 late promoter recognition protein gp55.Semantic proximity Read ↗

Modifications of the active center of T4 thioredoxin by site-directed mutagenesis.Semantic proximity Read ↗

Isolation of transcriptionally active mutants of T7 RNA polymerase that do not support phage growth.Semantic proximity Read ↗

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