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Article

Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.

Nucleic acids research - 11 Mar 2015

Holguera Isabel, Muñoz-Espín Daniel, Salas Margarita

Abstract excerpt

Phage ϕ29 DNA replication takes place by a protein-priming mechanism in which the viral DNA polymerase catalyses the covalent linkage of the initiating nucleotide to a specific serine residue of the terminal protein (TP). The N-terminal domain of the ϕ29 TP has been shown to bind to the host DNA in a sequence-independent manner and this binding is essential for the TP nucleoid localisation and for an efficient...

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Identifiers

PMID: 25722367
DOI: 10.1093/nar/gkv127
PMCID: PMC4357725

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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.

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Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.PMID 25722367Read ↗

Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid.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 ↗

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 ↗

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

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 ↗

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

ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.Semantic proximity Read ↗

Involvement of the "linker" region between the exonuclease and polymerization domains of phi29 DNA polymerase in DNA and TP binding.Semantic proximity Read ↗

Functional domain for priming activity in the phage phi 29 terminal protein.Semantic proximity Read ↗

The adenovirus priming protein pTP contributes to the kinetics of initiation of DNA replication.Semantic proximity Read ↗

phi29 DNA polymerase residue Phe128 of the highly conserved (S/T)Lx(2)h motif is required for a stable and functional interaction with the terminal protein.Semantic proximity Read ↗

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