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Article

Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly.

Journal of molecular biology - 5 Dec 1990

Bazinet C, Villafane R, King J

Abstract excerpt

The DNA packaging portal of the phage P22 procapsid is formed of 12 molecules of the 90,000 dalton gene 1 protein. The assembly of this dodecameric complex at a unique capsid vertex requires scaffolding subunits. The mechanism that ensures the location of the 12-fold symmetrical portal at only one of the 12 5-fold vertices of an icosahedral virus capsid presents a unique assembly problem, which, in some viruses,...

Topics

Alleles
Amino Acid Sequence
Base Sequence
Capsid
Cold Temperature
DNA, Viral
Kinetics
Molecular Sequence Data
Mutation
Phenotype
RNA, Viral
Salmonella Phages

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Suppression, Genetic

Temperature

Viral Core Proteins

Source

Identifiers

PMID: 2258936
DOI: 10.1016/0022-2836(90)90393-Z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2258936-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly.PMID 2258936Read ↗

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Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.Semantic proximity Read ↗

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