Evidence map›Paper›PMID 19109926›Full record

ArticleBiochemical and biophysical research communications2009

E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides.

Nikhil Jain, Neha Dhimole, Abu Rafay Khan, Debojyoti De, Sushil Kumar Tomar, Mathew Sajish, Dipak Dutta, Pradeep Parrack, Balaji Prakash

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Mycobacterial HflX is a ribosome splitting factor that mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Review
  8. Review
  9. HflXr, a homolog of a ribosome-splitting factor, mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. HflX protein protectsJournal of biosciences · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Nikhil JainDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016, India.
Neha Dhimole
Abu Rafay Khan
Debojyoti De
Sushil Kumar Tomar
Mathew Sajish
Dipak Dutta
Pradeep Parrack
Balaji Prakash
Indian Institute of Technology Kanpur · INBose Institute · IN

Funding

Wellcome Trust
6 · The paper itself

Abstract

HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage infection in Escherichia coli. We find that E. coli HflX binds 16S and 23S rRNA - the RNA components of 30S and 50S ribosomal subunits. Here, using purified ribosomal subunits, we show that HflX specifically interacts with the 50S. This finding is in line with the homology of HflX to GTPases involved in ribosome biogenesis. However, HflX-50S interaction is not limited to a specific nucleotide-bound state of the protein, and the presence of any of the nucleotides GTP/GDP/ATP/ADP is sufficient. In this respect, HflX is different from other GTPases. While E. coli HflX binds and hydrolyses both ATP and GTP, only the GTP hydrolysis activity is stimulated by 50S binding. This work uncovers interesting attributes of HflX in ribosome binding.

Indexed as

Adenosine TriphosphateAmino Acid SequenceCloning, MolecularEscherichia coliEscherichia coli ProteinsGTP-Binding ProteinsGuanosine TriphosphateHydrolysisMolecular Sequence DataNucleotidesRibosome Subunits, Large, BacterialAdenosine TriphosphateEscherichia coli ProteinsGTP-Binding ProteinsGuanosine TriphosphateHflX protein, E coliNucleotides

Identifiers

PMID19109926
PMCPMC2686079
OpenAlexW2048120284

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.