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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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Bibliografische gegevens
Hoofdauteurs: Wigneshweraraj, Siva R., Ishihama, Akira, Buck, Martin
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Oxford University Press 2001
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC29711/
https://ncbi.nlm.nih.gov/pubmed/11222766
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