ArticleGenes & development2013
Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.
Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Real-time capture of σNature communications · 2025Article
- Dissecting the multifaceted roles of autophagy in cancer initiation, growth, and metastasis: from molecular mechanisms to therapeutic applications.Medical oncology (Northwood, London, England) · 2024Review
- REC domain stabilizes the active heptamer of σiScience · 2023Article
- A general mechanism for transcription bubble nucleation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular Mechanism and Agricultural Application of the NifA-NifL System for Nitrogen Fixation.International journal of molecular sciences · 2023Review
- Mechanisms of DNA opening revealed in AAA+ transcription complex structures.Science advances · 2022Article
- SPARC: Structural properties associated with residue constraints.Computational and structural biotechnology journal · 2022Article
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- 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
- Bacterial Enhancer Binding Proteins-AAABiomolecules · 2020Review
- Mechanisms of σJournal of molecular biology · 2019Review
- Hexameric assembly of the AAA+ protein McrB is necessary for GTPase activity.Nucleic acids research · 2019Article
- Article
- Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Nucleic acids research · 2017Article
- Cryo-EM structures of the ATP-bound Vps4Nature communications · 2017Article
- Structures of RNA Polymerase Closed and Intermediate Complexes Reveal Mechanisms of DNA Opening and Transcription Initiation.Molecular cell · 2017Article
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase.Scientific reports · 2017Article
- Role of the σJournal of molecular biology · 2016Article
- Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF).Journal of molecular biology · 2016Review
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4 authors.
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Abstract
It is largely unknown how the typical homomeric ring geometry of ATPases associated with various cellular activities enables them to perform mechanical work. Small-angle solution X-ray scattering, crystallography, and electron microscopy (EM) reconstructions revealed that partial ATP occupancy caused the heptameric closed ring of the bacterial enhancer-binding protein (bEBP) NtrC1 to rearrange into a hexameric split ring of striking asymmetry. The highly conserved and functionally crucial GAFTGA loops responsible for interacting with σ54-RNA polymerase formed a spiral staircase. We propose that splitting of the ensemble directs ATP hydrolysis within the oligomer, and the ring's asymmetry guides interaction between ATPase and the complex of σ54 and promoter DNA. Similarity between the structure of the transcriptional activator NtrC1 and those of distantly related helicases Rho and E1 reveals a general mechanism in homomeric ATPases whereby complex allostery within the ring geometry forms asymmetric functional states that allow these biological motors to exert directional forces on their target macromolecules.
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