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The bacterial σ factors confer promoter specificity to the RNA polymerase (RNAP). One alternative σ factor, σ N , is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA + ATPases. We report a 3.4-Å resolution X-ray crystal structure of a σ N fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by σ N The structure allowed us to build and refine an improved σ N -holoenzyme model based on previously published 3.8-Å resolution X-ray data. The improved σ N -holoenzyme model reveals a conserved interdomain interface within σ N that, when disrupted by mutations, leads to transcription activity without activator intervention (so-called bypass mutants). Thus, the structure and stability of this interdomain interface are crucial for the role of σ N in blocking transcription activity and in maintaining the activator sensitivity of σ N .

Crystal structure of Aquifex aeolicus σ N bound to promoter DNA and the structure of σ N -holoenzyme

Crystal structure of Aquifex aeolicus σ ^N bound to promoter DNA and the structure of σ ^N -holoenzyme