Structures and mechanism of transcription initiation by bacterial ECF factors.
Bacterial Proteins
/ chemistry
Cryoelectron Microscopy
DNA, Bacterial
/ metabolism
Escherichia coli
/ genetics
Escherichia coli Proteins
/ chemistry
Models, Molecular
Mycobacterium tuberculosis
/ genetics
Nucleic Acid Conformation
Protein Conformation
Protein Interaction Mapping
Recombinant Fusion Proteins
/ chemistry
Sigma Factor
/ chemistry
Transcription Initiation, Genetic
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
26 07 2019
26 07 2019
Historique:
accepted:
17
05
2019
revised:
09
05
2019
received:
08
02
2019
pubmed:
28
5
2019
medline:
7
1
2020
entrez:
28
5
2019
Statut:
ppublish
Résumé
Bacterial RNA polymerase (RNAP) forms distinct holoenzymes with extra-cytoplasmic function (ECF) σ factors to initiate specific gene expression programs. In this study, we report a cryo-EM structure at 4.0 Å of Escherichia coli transcription initiation complex comprising σE-the most-studied bacterial ECF σ factor (Ec σE-RPo), and a crystal structure at 3.1 Å of Mycobacterium tuberculosis transcription initiation complex with a chimeric σH/E (Mtb σH/E-RPo). The structure of Ec σE-RPo reveals key interactions essential for assembly of E. coli σE-RNAP holoenzyme and for promoter recognition and unwinding by E. coli σE. Moreover, both structures show that the non-conserved linkers (σ2/σ4 linker) of the two ECF σ factors are inserted into the active-center cleft and exit through the RNA-exit channel. We performed secondary-structure prediction of 27,670 ECF σ factors and find that their non-conserved linkers probably reach into and exit from RNAP active-center cleft in a similar manner. Further biochemical results suggest that such σ2/σ4 linker plays an important role in RPo formation, abortive production and promoter escape during ECF σ factors-mediated transcription initiation.
Identifiants
pubmed: 31131408
pii: 5498757
doi: 10.1093/nar/gkz470
pmc: PMC6648896
doi:
Substances chimiques
Bacterial Proteins
0
DNA, Bacterial
0
Escherichia coli Proteins
0
Recombinant Fusion Proteins
0
Sigma Factor
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7094-7104Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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