CueR activates transcription through a DNA distortion mechanism.
Nat Chem Biol
; 17(1): 57-64, 2021 01.
Article
en En
| MEDLINE
| ID: mdl-32989300
ABSTRACT
The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprising Escherichia coli CueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
ARN Polimerasas Dirigidas por ADN
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ADN Bacteriano
/
Regulación Bacteriana de la Expresión Génica
/
Transactivadores
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Proteínas de Escherichia coli
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Proteínas de Unión al ADN
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Escherichia coli
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Nat Chem Biol
Asunto de la revista:
BIOLOGIA
/
QUIMICA
Año:
2021
Tipo del documento:
Article
País de afiliación:
China