DNA Binding of PhoB and its Interaction with RNA Polymerase

We have identified the DNA-binding domain (DBD) of an Escherichia coliactivator 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 σ 70subunit. Assuming that the PhoB DBD is st...

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Veröffentlicht in:	Journal of molecular biology 1996-05, Vol.259 (1), p.15-26
Hauptverfasser:	Makino, Kozo, Amemura, Mitsuko, Kawamoto, Takeshi, Kimura, Sigenobu, Shinagawa, Hideo, Nakata, Atsuo, Suzuki, Masashi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Binding Sites Carrier Proteins - chemistry Carrier Proteins - genetics DNA bending DNA recognition DNA, Bacterial - chemistry DNA, Bacterial - metabolism DNA-Directed RNA Polymerases - metabolism Electrophoresis - methods Escherichia coli Escherichia coli - chemistry Escherichia coli Proteins gene regulation histone H5 Membrane Proteins - chemistry Membrane Proteins - genetics Models, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation Periplasmic Binding Proteins Phosphate-Binding Proteins Promoter Regions, Genetic Protein Binding Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Deletion Sequence Homology, Amino Acid sigma factor
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