ArticleGenes & development2003
Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains.
Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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102 citing papers in PubMed.
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- Subunit specialization in AAA+ proteins and substrate unfolding during transcription complex remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Detection of environmental pollutants using transcription factor-based whole-cell biosensors.Biotechnology for the environment · 2025Review
- Flip the switch: the role of FleQ in modulating the transition between the free-living and sessile mode of growth inJournal of bacteriology · 2024Review
- Identification of critical amino acids in the DNA binding domain of LuxO: Lessons from a constitutive active LuxO.PloS one · 2024Article
- REC domain stabilizes the active heptamer of σiScience · 2023Article
- Structure of phosphorylated-like RssB, the adaptor delivering σThe Journal of biological chemistry · 2023Article
- Subtle sequence differences between two interacting σThe FEBS journal · 2022Article
- Cooperativity in ATP Hydrolysis by MopR Is Modulated by Its Signal Reception Domain and by Its Protein and Phenol Concentrations.Journal of bacteriology · 2022Article
- SPARC: Structural properties associated with residue constraints.Computational and structural biotechnology journal · 2022Article
- The heptameric structure of the flagellar regulatory protein FlrC is indispensable for ATPase activity and disassembled by cyclic-di-GMP.The Journal of biological chemistry · 2020Article
- The Response ofmBio · 2020Article
- Tetrameric architecture of an active phenol-bound form of the AAANature communications · 2020Article
- Bacterial Enhancer Binding Proteins-AAABiomolecules · 2020Review
- New Insights into Multistep-Phosphorelay (MSP)/ Two-Component System (TCS) Regulation: Are Plants and Bacteria that Different?Plants (Basel, Switzerland) · 2019Review
- Mechanisms of σJournal of molecular biology · 2019Review
- Suppressor mutations reveal an NtrC-like response regulator, NmpR, for modulation of Type-IV Pili-dependent motility in Myxococcus xanthus.PLoS genetics · 2018Article
- Cryo-EM structures of the human INO80 chromatin-remodeling complex.Nature structural & molecular biology · 2018Article
- Towards quantitative analysis of gene regulation by enhancers.Epigenomics · 2017Review
- Structures of RNA Polymerase Closed and Intermediate Complexes Reveal Mechanisms of DNA Opening and Transcription Initiation.Molecular cell · 2017Article
42 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
Transcription by sigma54 RNA polymerase depends on activators that contain ATPase domains of the AAA+ class. These activators, which are often response regulators of two-component signal transduction systems, remodel the polymerase so that it can form open complexes at promoters. Here, we report the first crystal structures of the ATPase domain of an activator, the NtrC1 protein from the extreme thermophile Aquifex aeolicus. This domain alone, which is active, crystallized as a ring-shaped heptamer. The protein carrying both the ATPase and adjacent receiver domains, which is inactive, crystallized as a dimer. In the inactive dimer, one residue needed for catalysis is far from the active site, and extensive contacts among the domains prevent oligomerization of the ATPase domain. Oligomerization, which completes the active site, depends on surfaces that are buried in the dimer, and hence, on a rearrangement of the receiver domains upon phosphorylation. A motif in the ATPase domain known to be critical for coupling energy to remodeling of polymerase forms a novel loop that projects from the middle of an alpha helix. The extended, structured loops from the subunits of the heptamer localize to a pore in the center of the ring and form a surface that could contact sigma54.
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