In vitro roles of invariant helix–turn–helix motif residue R383 in σ(54) (σ(N))

In vitro DNA-binding and transcription properties of σ(54) proteins with the invariant Arg383 in the putative helix–turn–helix motif of the DNA-binding domain substituted by lysine or alanine are described. We show that R383 contributes to maintaining stable holoenzyme–promoter complexes in which li...

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Detalhes bibliográficos

Publicado no:	Nucleic Acids Res
Principais autores:	Wigneshweraraj, Siva R., Ishihama, Akira, Buck, Martin
Formato:	Artigo
Idioma:	Inglês
Publicado em:	Oxford University Press 2001
Assuntos:	Article
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC29711/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11222766/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/29.5.1163
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