Evidence map›Paper›PMID 19706445›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.

Chao Tu, Xiaomei Zhou, Joseph E Tropea, Brian P Austin, David S Waugh, Donald L Court, Xinhua Ji

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

55 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Comparative Analysis of anti-Shine- Dalgarno Function inFrontiers in molecular biosciences · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019
    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

7 authors at 3 institutions in 1 country.

Chao TuCenter for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Xiaomei Zhou
Joseph E Tropea
Brian P Austin
David S Waugh
Donald L Court
Xinhua Ji
National Institutes of Health · USCenter for Cancer Research · USNational Cancer Institute · US

Funding

Biomolecular Structure and Mechanism, Structure-Based Drug DesignZIABC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2009 to 2024
$27.3M
Lambda Genetic Networks and Lambda Red-Mediated RecombinationZIABC010336 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI COURT, DONALD · 2009 to 2020
$18.9M
Protein Purification CoreZICBC011016 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI TROPEA, JOSEPH · 2009 to 2021
$11.0M
Intramural NIH HHS
6 · The paper itself

Abstract

ERA, composed of an N-terminal GTPase domain followed by an RNA-binding KH domain, is essential for bacterial cell viability. It binds to 16S rRNA and the 30S ribosomal subunit. However, its RNA-binding site, the functional relationship between the two domains, and its role in ribosome biogenesis remain unclear. We have determined two crystal structures of ERA, a binary complex with GDP and a ternary complex with a GTP-analog and the 1531AUCACCUCCUUA1542 sequence at the 3' end of 16S rRNA. In the ternary complex, the first nine of the 12 nucleotides are recognized by the protein. We show that GTP binding is a prerequisite for RNA recognition by ERA and that RNA recognition stimulates its GTP-hydrolyzing activity. Based on these and other data, we propose a functional cycle of ERA, suggesting that the protein serves as a chaperone for processing and maturation of 16S rRNA and a checkpoint for assembly of the 30S ribosomal subunit. The AUCA sequence is highly conserved among bacteria, archaea, and eukaryotes, whereas the CCUCC, known as the anti-Shine-Dalgarno sequence, is conserved in noneukaryotes only. Therefore, these data suggest a common mechanism for a highly conserved ERA function in all three kingdoms of life by recognizing the AUCA, with a "twist" for noneukaryotic ERA proteins by also recognizing the CCUCC.

Indexed as

Amino Acid SequenceBacteriaConserved SequenceCrystallography, X-RayGTP PhosphohydrolasesGuanosine TriphosphateModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibosomesRNA, Ribosomal, 16SSequence AlignmentGTP PhosphohydrolasesGuanosine TriphosphateRNA, Ribosomal, 16S

Identifiers

PMID19706445
PMCPMC2736428
OpenAlexW2113545203

What OpenQuestion holds

Textmetadata
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.