ArticleProceedings of the National Academy of Sciences of the United States of America2010
A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 29 citations in OpenAlex.
- The RNA repair proteins RtcAB regulate transcription activator RtcR via its CRISPR-associated Rossmann fold domain.iScience · 2022Article
- Bacterial Enhancer Binding Proteins-AAABiomolecules · 2020Review
- Structural basis of transcription inhibition by the DNA mimic protein Ocr of bacteriophage T7.eLife · 2020Article
- Mechanisms of σJournal of molecular biology · 2019Review
- Structures of Bacterial RNA Polymerase Complexes Reveal the Mechanism of DNA Loading and Transcription Initiation.Molecular cell · 2018Article
- 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
- Genome wide interactions of wild-type and activator bypass forms of σ54.Nucleic acids research · 2015Article
- Article
- A perspective on the enhancer dependent bacterial RNA polymerase.Biomolecules · 2015Review
- Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA+ activator.Nucleic acids research · 2014Article
- Nitrogen stress response and stringent response are coupled in Escherichia coli.Nature communications · 2014Article
- Domain movements of the enhancer-dependent sigma factor drive DNA delivery into the RNA polymerase active site: insights from single molecule studies.Nucleic acids research · 2014Article
- Transcriptional control by two interacting regulatory proteins: identification of the PtxS binding site at PtxR.Nucleic acids research · 2013Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
- An aromatic residue switch in enhancer-dependent bacterial RNA polymerase controls transcription intermediate complex activity.Nucleic acids research · 2013Article
- A dual switch controls bacterial enhancer-dependent transcription.Nucleic acids research · 2012Article
- A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements.Nucleic acids research · 2012Article
- The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription.Microbiology and molecular biology reviews : MMBR · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ATP hydrolysis-dependent molecular machines and motors often drive regulated conformational transformations in cell signaling and gene regulation complexes. Conformational reorganization of a gene regulation complex containing the major variant form of bacterial RNA polymerase (RNAP), Esigma(54), requires engagement with its cognate ATP-hydrolyzing activator protein. Importantly, this activated RNAP is essential for a number of adaptive responses, including those required for bacterial pathogenesis. Here we characterize the initial encounter between the enhancer-dependent Esigma(54) and its cognate activator AAA+ ATPase protein, before ADP+P(i) formation, using a small primed RNA (spRNA) synthesis assay. The results show that in a prehydrolysis state, sufficient activator-dependent rearrangements in Esigma(54) have occurred to allow engagement of the RNAP active site with single-stranded promoter DNA to support spRNA synthesis, but not to melt the promoter DNA. This catalytically competent transcription intermediate has similarity with the open promoter complex, in that the RNAP dynamics required for DNA scrunching should be occurring. Significantly, this work highlights that prehydrolysis states of ATPases are functionally important in the molecular transformations they drive.
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