Evidence map›Paper›PMID 26610483›Full record

ArticleInternational journal of molecular sciences2015

Nucleotide-Induced Conformational Changes in Escherichia coli DnaA Protein Are Required for Bacterial ORC to Pre-RC Conversion at the Chromosomal Origin.

Rahul Saxena, Sona Vasudevan, Digvijay Patil, Norah Ashoura, Julia E Grimwade, Elliott Crooke

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. IHF and Fis asInternational journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. The DnaA Cycle inFrontiers in microbiology · 2017
    Review
  10. Article
  11. Review
  12. Review
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

6 authors at 3 institutions in 1 country.

Rahul SaxenaDepartment of Biochemistry and Molecular & Cellular Biology Georgetown University Medical Center, Washington, DC 20007, USA. rs426@georgetown.edu.
Sona VasudevanDepartment of Biochemistry and Molecular & Cellular Biology Georgetown University Medical Center, Washington, DC 20007, USA. sv67@georgetown.edu.
Digvijay PatilDepartment of Biochemistry and Molecular & Cellular Biology Georgetown University Medical Center, Washington, DC 20007, USA. dap89@georgetown.edu.
Norah AshouraDepartment of Biological Sciences, Florida Institute of Technology, 150 West University Blvd, Melbourne, FL 32901, USA. nashoura2010@utexas.edu.
Julia E GrimwadeDepartment of Biological Sciences, Florida Institute of Technology, 150 West University Blvd, Melbourne, FL 32901, USA. grimwade@fit.edu.
Elliott CrookeDepartment of Biochemistry and Molecular & Cellular Biology Georgetown University Medical Center, Washington, DC 20007, USA. crooke@georgetown.edu.
Florida Institute of Technology · USGeorgetown University · USGeorgetown University Medical Center · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
Membranes in the Initiation of Chromsomal ReplicationR01GM049700 · NIGMS · GEORGETOWN UNIVERSITY · PI CROOKE, ELLIOTT · 1994 to 2010
$2.7M
CELL CYCLE ASSEMBLY OF NUCLEOPROTEIN COMPLEXESR01GM054042 · NIGMS · FLORIDA INSTITUTE OF TECHNOLOGY · PI LEONARD, ALAN CARL · 1997 to 2013
$2.6M
MEMBRANES IN THE INITIATION OF CHROMOSOMAL REPLICATIONR21GM049700 · NIGMS · GEORGETOWN UNIVERSITY · PI CROOKE, ELLIOTT · 1994 to 1996
–
NCI NIH HHS P30 CA051008NCI NIH HHS P30-CA051008NIGMS NIH HHS GM49700NIGMS NIH HHS GM54042NIGMS NIH HHS R01 GM049700NIGMS NIH HHS R01 GM054042
6 · The paper itself

Abstract

DnaA oligomerizes when bound to origins of chromosomal replication. Structural analysis of a truncated form of DnaA from Aquifex aeolicus has provided insight into crucial conformational differences within the AAA+ domain that are specific to the ATP- versus ADP- bound form of DnaA. In this study molecular docking of ATP and ADP onto Escherichia coli DnaA, modeled on the crystal structure of Aquifex aeolicus DnaA, reveals changes in the orientation of amino acid residues within or near the vicinity of the nucleotide-binding pocket. Upon limited proteolysis with trypsin or chymotrypsin ADP-DnaA, but not ATP-DnaA generated relatively stable proteolytic fragments of various sizes. Examined sites of limited protease susceptibility that differ between ATP-DnaA and ADP-DnaA largely reside in the amino terminal half of DnaA. The concentration of adenine nucleotide needed to induce conformational changes, as detected by these protease susceptibilities of DnaA, coincides with the conversion of an inactive bacterial origin recognition complex (bORC) to a replication efficient pre-replication complex (pre-RC) at the E. coli chromosomal origin of replication (oriC).

Indexed as

Chromosomes, BacterialOrigin Recognition ComplexProtein ConformationReplication OriginAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsBinding SitesCarbohydrate ConformationDNA-Binding ProteinsDNA ReplicationEscherichia coliModels, MolecularNucleoproteinsNucleotidesProtein BindingAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsDnaA protein, BacteriaDNA-Binding ProteinsNucleoproteinsNucleotidesOrigin Recognition ComplexAAA+ domainchromosomal originDnaA proteinDNA replicationmolecular dockingproteolysis

Identifiers

PMID26610483
PMCPMC4661922
OpenAlexW2173910572

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.