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Article

DNA binding of PhoB and its interaction with RNA polymerase.

Journal of molecular biology - 31 May 1996

Makino K, Amemura M, Kawamoto T, Kimura S, Shinagawa H, Nakata A, Suzuki M

Abstract excerpt

We have identified the DNA-binding domain (DBD) of an Escherichia coli activator protein PhoB as its C-terminal 91 residues. Four amino acid positions in the PhoB DBD are found important for interaction with the RNA polymerase holoenzyme that contains the sigma 70 subunit. Assuming that the PhoB DBD is structurally similar to the histone H5 DBD, the four positions are placed around the turn region that connects...

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Identifiers

PMID: 8648643
DOI: 10.1006/jmbi.1996.0298

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Research trail→

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DNA binding of PhoB and its interaction with RNA polymerase.PMID 8648643Read ↗

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Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the regulatory gene for the phosphate regulon.Semantic proximity Read ↗

Minor groove recognition is important for the transcription factor PhoB: a surface plasmon resonance study.Semantic proximity Read ↗

The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation.Semantic proximity Read ↗

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Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase.Semantic proximity Read ↗

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