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Article

Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segments.

Journal of bacteriology - 1 Feb 1997

Donner A L, Carlson P A, Koudelka G B

Abstract excerpt

The repressor protein of bacteriophage P22 binds to DNA as a homodimer. This dimerization is absolutely required for DNA binding. Dimerization is mediated by interactions between amino acids in the carboxyl (C)-terminal domain. We have constructed a plasmid, p22CT-1, which directs the overproduction of just the C-terminal domain of the P22 repressor (P22CT-1). Addition of P22CT-1 to DNA-bound P22 repressor causes...

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Identifiers

PMID: 9023209
DOI: 10.1128/jb.179.4.1253-1261.1997
PMCID: PMC178823

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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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