Evidence map›Paper›PMID 19486295›Full record

ArticleMolecular microbiology2009

Functional roles of the pre-sensor I insertion sequence in an AAA+ bacterial enhancer binding protein.

Patricia C Burrows, Jörg Schumacher, Samuel Amartey, Tamaswati Ghosh, Timothy A Burgis, Xiaodong Zhang, B Tracy Nixon, Martin Buck

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms of σJournal of molecular biology · 2019
    Review
  4. Review
  5. Article
  6. Article
  7. A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Patricia C BurrowsDepartment of Life Sciences, Division of Biology, Imperial College London, London, UK.
Jörg Schumacher
Samuel Amartey
Tamaswati Ghosh
Timothy A Burgis
Xiaodong Zhang
B Tracy Nixon
Martin Buck
GTx (United States) · USEquilibrium Research · GBImperial College London · GBPennsylvania State University · US

Funding

Elucidating the Conformational Dynamics of the AAA+ ATPases NtrC1 and NtrCR01GM069937 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI NIXON, B TRACY · 2006 to 2009
$1.3M
Biotechnology and Biological Sciences Research Council BB/G020434/1NIGMS NIH HHS GM069937NIGMS NIH HHS R01 GM069937Wellcome Trust
6 · The paper itself

Abstract

Molecular machines belonging to the AAA+ superfamily of ATPases use NTP hydrolysis to remodel their versatile substrates. The presence of an insertion sequence defines the major phylogenetic pre-sensor I insertion (pre-SIi) AAA+ superclade. In the bacterial sigma(54)-dependent enhancer binding protein phage shock protein F (PspF) the pre-SIi loop adopts different conformations depending on the nucleotide-bound state. Single amino acid substitutions within the dynamic pre-SIi loop of PspF drastically change the ATP hydrolysis parameters, indicating a structural link to the distant hydrolysis site. We used a site-specific protein-DNA proximity assay to measure the contribution of the pre-SIi loop in sigma(54)-dependent transcription and demonstrate that the pre-SIi loop is a major structural feature mediating nucleotide state-dependent differential engagement with Esigma(54). We suggest that much, if not all, of the action of the pre-SIi loop is mediated through the L1 loop and relies on a conserved molecular switch, identified in a crystal structure of one pre-SIi variant and in accordance with the high covariance between some pre-SIi residues and distinct residues outside the pre-SIi sequence.

Indexed as

Mutagenesis, InsertionalAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SubstitutionEscherichia coliEscherichia coli ProteinsHydrolysisProtein Structure, TertiaryRNA Polymerase Sigma 54Trans-ActivatorsTranscriptional ActivationAdenosine TriphosphatasesAdenosine TriphosphateEscherichia coli ProteinsPspF protein, E coliRNA Polymerase Sigma 54rpoN protein, E coliTrans-Activators

Identifiers

PMID19486295
PMCPMC2745333
OpenAlexW2134862417

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.