ArticleBiopolymers2013
Structure, function, and tethering of DNA-binding domains in σ⁵⁴ transcriptional activators.
Article in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The response regulator BqsR/CarR controls FeNature communications · 2026Article
- KLF5 enables dichotomous lineage programs in pancreatic cancer via the AAA+ ATPase coactivators RUVBL1 and RUVBL2.Nature communications · 2025Article
- Association ofBiomedicines · 2023Article
- Purification and Biochemical Characterization of the DNA Binding Domain of the Nitrogenase Transcriptional Activator NifA from Gluconacetobacter diazotrophicus.The protein journal · 2023Article
- Subtle sequence differences between two interacting σThe FEBS journal · 2022Article
- RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression.PLoS pathogens · 2020Article
- Bacterial Enhancer Binding Proteins-AAABiomolecules · 2020Review
- The Azoarcus anaerobius 1,3-Dihydroxybenzene (Resorcinol) Anaerobic Degradation Pathway Is Controlled by the Coordinated Activity of Two Enhancer-Binding Proteins.Applied and environmental microbiology · 2017Article
- Kinetics of transcription initiation directed by multiple cis-regulatory elements on the glnAp2 promoter.Nucleic acids research · 2016Article
- Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- σ54-dependent regulome in Desulfovibrio vulgaris Hildenborough.BMC genomics · 2015Article
- DNA recognition by a σ(54) transcriptional activator from Aquifex aeolicus.Journal of molecular biology · 2014Article
- Crystallization and preliminary X-ray analysis of the ATPase domain of the σ(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.Genes & development · 2013Article
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7 authors.
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Abstract
We compare the structure, activity, and linkage of DNA-binding domains (DBDs) from σ(54) transcriptional activators and discuss how the properties of the DBDs and the linker to the neighboring domain are affected by the overall properties and requirements of the full proteins. These transcriptional activators bind upstream of specific promoters that utilize σ(54)-polymerase. Upon receiving a signal the activators assemble into hexamers, which then, through adenosine triphosphate (ATP) hydrolysis, drive a conformational change in polymerase that enables transcription initiation. We present structures of the DBDs of activators nitrogen regulatory protein C 1 (NtrC1) and Nif-like homolog 2 (Nlh2) from the thermophile Aquifex aeolicus. The structures of these domains and their relationship to other parts of the activators are discussed. These structures are compared with previously determined structures of the DBDs of NtrC4, NtrC, ZraR, and factor for inversion stimulation. The N-terminal linkers that connect the DBDs to the central domains in NtrC1 and Nlh2 were studied and found to be unstructured. Additionally, a crystal structure of full-length NtrC1 was solved, but density of the DBDs was extremely weak, further indicating that the linker between ATPase and DBDs functions as a flexible tether. Flexible linking of ATPase and DBDs is likely necessary to allow assembly of the active hexameric ATPase ring. The comparison of this set of activators also shows clearly that strong dimerization of the DBD only occurs when other domains do not dimerize strongly.
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