Details
- Autor(en) / Beteiligte
- Titel
- Crl activates transcription by stabilizing active conformation of the master stress transcription initiation factor
- Ist Teil von
- eLife, 2019-12, Vol.8
- Ort / Verlag
- England: eLife Sciences Publications Ltd
- Erscheinungsjahr
- 2019
- Link zum Volltext
- Quelle
- Free E-Journal (出版社公開部分のみ）
- Beschreibungen/Notizen
- σ is a master transcription initiation factor that protects bacterial cells from various harmful environmental stresses including antibiotic pressure. Although its mechanism remains unclear, it is known that full activation of σ -mediated transcription requires a σ -specific activator, Crl. In this study, we determined a 3.80 Å cryo-EM structure of an transcription activation complex ( Crl-TAC) comprising σ -RNA polymerase (σ -RNAP) holoenzyme, Crl, and a nucleic-acid scaffold. The structure reveals that Crl interacts with domain 2 of σ (σ ) and the RNAP core enzyme, but does not contact promoter DNA. Results from subsequent hydrogen-deuterium exchange mass spectrometry (HDX-MS) indicate that Crl stabilizes key structural motifs within σ to promote the assembly of the σ -RNAP holoenzyme and also to facilitate formation of an RNA polymerase-promoter DNA open complex (RPo). Our study demonstrates a unique DNA contact-independent mechanism of transcription activation, thereby defining a previously unrecognized mode of transcription activation in cells.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2050-084XeISSN: 2050-084XDOI: 10.7554/eLife.50928Titel-ID: cdi_doaj_primary_oai_doaj_org_article_7d66de756fe24a4bb02c35d7ddf80c6d
- Format
- –
- Schlagworte
- Amino Acid Sequence, Antibiotics, Biofilms, Cell activation, Cell adhesion & migration, Chromosomes and Gene Expression, Conformation, Crl, Cryoelectron Microscopy, Deoxyribonucleic acid, DNA, DNA-directed RNA polymerase, DNA-Directed RNA Polymerases - chemistry, DNA-Directed RNA Polymerases - metabolism, E coli, Enzymes, Escherichia coli - metabolism, Escherichia coli Proteins - chemistry, Escherichia coli Proteins - metabolism, Escherichia coli Proteins - ultrastructure, Hydrogen-deuterium exchange, Interfaces, Mass spectroscopy, Models, Molecular, NMR, Nuclear magnetic resonance, Protein Binding, Protein Conformation, Protein Stability, RNA polymerase, Salmonella, sigma factor, Sigma Factor - chemistry, Sigma Factor - metabolism, Sigma Factor - ultrastructure, stress response, Transcription activation, transcription factors, Transcription Factors - chemistry, Transcription Factors - metabolism, Transcription Factors - ultrastructure, Transcription, Genetic