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

Functional domain for priming activity in the phage phi 29 terminal protein.

Gene - 30 Mar 1990

Garmendia C, Hermoso J M, Salas M

Abstract excerpt

By site-directed mutagenesis we have changed into Cys the Ser232 of the phi 29 terminal protein (TP) involved in the covalent linkage to dAMP for the initiation of replication. The mutant TP, highly purified, had about 0.7% of the priming activity of the wild-type (wt) protein p3. The linkage between the mutant protein p3 and dAMP was more labile to piperidine treatment than the serine-dAMP linkage in the wt...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacteriophages
Share to DNA-Directed DNA Polymerase

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

Share to DNA Replication

Share to Molecular Sequence Data

Share to Mutation

Share to Viral Proteins

Source

Identifiers

PMID: 2341040
DOI: 10.1016/0378-1119(90)90061-u

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

Functional domain for priming activity in the phage phi 29 terminal protein.PMID 2341040Read ↗

Involvement of residues of the 29 terminal protein intermediate and priming domains in the formation of a stable and functional heterodimer with the replicative DNA polymerase.Semantic proximity Read ↗

An aspartic acid residue in TPR-1, a specific region of protein-priming DNA polymerases, is required for the functional interaction with primer terminal protein.Semantic proximity Read ↗

A highly conserved lysine residue in phi29 DNA polymerase is important for correct binding of the templating nucleotide during initiation of phi29 DNA replication.Semantic proximity Read ↗

Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.Semantic proximity Read ↗

phi29 DNA polymerase-terminal protein interaction. Involvement of residues specifically conserved among protein-primed DNA polymerases.Semantic proximity Read ↗

Involvement of the TPR2 subdomain movement in the activities of phi29 DNA polymerase.Semantic proximity Read ↗

Two positively charged residues of phi29 DNA polymerase, conserved in protein-primed DNA polymerases, are involved in stabilisation of the incoming nucleotide.Semantic proximity Read ↗

A conserved insertion in protein-primed DNA polymerases is involved in primer terminus stabilisation.Semantic proximity Read ↗

Mechanism of stimulation of DNA replication by bacteriophage phi 29 single-stranded DNA-binding protein p5Semantic proximity Read ↗

The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization.Semantic proximity Read ↗

Functional linkages between replication proteins of genes 1, 3 and 5 of Bacillus subtilis phage φ29.Semantic proximity Read ↗

A Mutation in the C-terminal domain of the RNA polymerase alpha subunit that destabilizes the open complexes formed at the phage phi 29 late A3 promoter.Semantic proximity Read ↗

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