Structural and functional insights into transcription activation of the essential LysR-type transcriptional regulators.
Escherichia coli
/ genetics
DNA-Directed RNA Polymerases
/ metabolism
Transcriptional Activation
Bacterial Proteins
/ chemistry
Promoter Regions, Genetic
Cryoelectron Microscopy
Escherichia coli Proteins
/ chemistry
Transcription Factors
/ chemistry
Models, Molecular
Molecular Docking Simulation
Gene Expression Regulation, Bacterial
Protein Multimerization
Binding Sites
C‐terminal domain of α subunit
GcvA_DBD
LTTR‐dependent transcription activation complex
LysR‐type transcriptional regulators (LTTRs)
RNA polymerase
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
Jun 2024
Jun 2024
Historique:
revised:
17
04
2024
received:
30
11
2023
accepted:
23
04
2024
medline:
10
5
2024
pubmed:
10
5
2024
entrez:
9
5
2024
Statut:
ppublish
Résumé
The enormous LysR-type transcriptional regulators (LTTRs), which are diversely distributed amongst prokaryotes, play crucial roles in transcription regulation of genes involved in basic metabolic pathways, virulence and stress resistance. However, the precise transcription activation mechanism of these genes by LTTRs remains to be explored. Here, we determine the cryo-EM structure of a LTTR-dependent transcription activation complex comprising of Escherichia coli RNA polymerase (RNAP), an essential LTTR protein GcvA and its cognate promoter DNA. Structural analysis shows two N-terminal DNA binding domains of GcvA (GcvA_DBD) dimerize and engage the GcvA activation binding sites, presenting the -35 element for specific recognition with the conserved σ
Substances chimiques
DNA-Directed RNA Polymerases
EC 2.7.7.6
Bacterial Proteins
0
LysR protein, Bacteria
87609-37-8
Escherichia coli Proteins
0
Transcription Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e5012Subventions
Organisme : National Natural Science Foundation of China
ID : 32270192
Organisme : National Natural Science Foundation of China
ID : 32270037
Organisme : National Natural Science Foundation of China
ID : 82072240
Organisme : National Natural Science Foundation of China
ID : 32000025
Organisme : National Natural Science Foundation of China
ID : 12004420
Organisme : National Natural Science Foundation of China
ID : 32071228
Organisme : Natural Science Foundation of Jiangsu Province
ID : BK20211302
Organisme : National Key R&D Program of China
ID : 2023YFC2308200
Organisme : Chinese Materia Medica First-Class Discipline of Nanjing University of Chinese Medicine
ID : 2020YLXK008
Organisme : Chinese Materia Medica First-Class Discipline of Nanjing University of Chinese Medicine
ID : 2020YLXK016
Organisme : Fok Ying Tung Education Foundation
Organisme : State Key Laboratory of Bioreactor Engineering
Organisme : East China University of Science and Technology
Organisme : Strategic Priority Research Program of the Chinese Academy of Sciences
ID : XDB37000000
Organisme : Youth Innovation Promotion Association of CAS
ID : 2021009
Informations de copyright
© 2024 The Protein Society.
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