ArticleNucleic acids research2012
A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- 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
- The bacterial enhancer-dependent RNA polymerase.The Biochemical journal · 2016Review
- Mutations in RNA Polymerase Bridge Helix and Switch Regions Affect Active-Site Networks and Transcript-Assisted Hydrolysis.Journal of molecular biology · 2015Article
- A perspective on the enhancer dependent bacterial RNA polymerase.Biomolecules · 2015Review
- Unique ATPase site architecture triggers cis-mediated synchronized ATP binding in heptameric AAA+-ATPase domain of flagellar regulatory protein FlrC.The Journal of biological chemistry · 2015Article
- Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.Genes & development · 2013Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Initiation of σ(54)-dependent transcription requires assistance to melt DNA at the promoter site but is impeded by numerous protein-protein and nucleo-protein interactions. To alleviate these inhibitory interactions, hexameric bacterial enhancer binding proteins (bEBP), a subset of the ATPases associated with various cellular activities (AAA+) protein family, are required to remodel the transcription complex using energy derived from ATP hydrolysis. However, neither the process of energy conversion nor the internal architecture of the closed promoter complex is well understood. Escherichia coli Phage shock protein F (PspF), a well-studied bEBP, contains a surface-exposed loop 1 (L1). L1 is key to the energy coupling process by interacting with Region I of σ(54) (σ(54)(RI)) in a nucleotide dependent manner. Our analyses uncover new levels of complexity in the engagement of a multimeric bEBP with a basal transcription complex via several L1s. The mechanistic implications for these multivalent L1 interactions are elaborated in the light of available structures for the bEBP and its target complexes.
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