Mechanisms of DNA opening revealed in AAA+ transcription complex structures.
Sci Adv
; 8(51): eadd3479, 2022 12 21.
Article
em En
| MEDLINE
| ID: mdl-36542713
ABSTRACT
Gene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on σ factors for its promoter specificities. Using a special form of sigma factor (σ54), which forms a stable closed complex and requires its activator that belongs to the AAA+ ATPases (ATPases associated with diverse cellular activities), we obtained cryo-electron microscopy structures of transcription initiation complexes that reveal a previously unidentified process of DNA melting opening. The σ54 amino terminus threads through the locally opened up DNA and then becomes enclosed by the AAA+ hexameric ring in the activator-bound intermediate complex. Our structures suggest how ATP hydrolysis by the AAA+ activator could remove the σ54 inhibition while helping to open up DNA, using σ54 amino-terminal peptide as a pry bar.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
RNA Polimerases Dirigidas por DNA
/
DNA
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article