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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Oxford University Press
2001
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC29711/ https://ncbi.nlm.nih.gov/pubmed/11222766 |
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