2019
DOI: 10.1002/prot.25768
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Structural basis for −35 element recognition by σ4 chimera proteins and their interactions with PmrA response regulator

Abstract: In class II transcription activation, the transcription factor normally binds to the promoter near the −35 position and contacts the domain 4 of σ factors (σ4) to activate transcription. However, σ4 of σ70 appears to be poorly folded on its own. Here, by fusing σ4 with the RNA polymerase β‐flap‐tip‐helix, we constructed two σ4 chimera proteins, one from σ70 ()σ470normalc and another from σS ()σ4Snormalc of Klebsiella pneumoniae. The two chimera proteins well folded into a monomeric form with strong binding aff… Show more

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