Evidence map›Paper›PMID 21726564›Full record

ArticleJournal of molecular biology2011

Two-step aminoacylation of tRNA without channeling in Archaea.

Hari Bhaskaran, John J Perona

Erratum issuedAbstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 19% 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, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  4. Elements of the cellular metabolic structure.Frontiers in molecular biosciences · 2015
    Article
  5. Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Article
  7. Emergence and evolution.Topics in current chemistry · 2014
    Review
  8. Article
  9. Article
  10. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Hari BhaskaranDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510, USA.
John J Perona
University of California, Santa Barbara · US

Funding

Specificity in the Synthesis of Aminoacyl-tRNAR01GM063713 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PERONA, JOHN J. · 2001 to 2012
$3.2M
NIGMS NIH HHS GM63713NIGMS NIH HHS R01 GM063713
6 · The paper itself

Abstract

Catalysis of sequential reactions is often envisaged to occur by channeling of substrate between enzyme active sites without release into bulk solvent. However, while there are compelling physiological rationales for direct substrate transfer, proper experimental support for the hypothesis is often lacking, particularly for metabolic pathways involving RNA. Here, we apply transient kinetics approaches developed to study channeling in bienzyme complexes to an archaeal protein synthesis pathway featuring the misaminoacylated tRNA intermediate Glu-tRNA(Gln). Experimental and computational elucidation of a kinetic and thermodynamic framework for two-step cognate Gln-tRNA(Gln) synthesis demonstrates that the misacylating aminoacyl-tRNA synthetase (GluRS(ND)) and the tRNA-dependent amidotransferase (GatDE) function sequentially without channeling. Instead, rapid processing of the misacylated tRNA intermediate by GatDE and preferential elongation factor binding to the cognate Gln-tRNA(Gln) together permit accurate protein synthesis without formation of a binary protein-protein complex between GluRS(ND) and GatDE. These findings establish an alternate paradigm for protein quality control via two-step pathways for cognate aminoacyl-tRNA formation.

Indexed as

Transfer RNA AminoacylationArchaeaBinding SitesCrystallography, X-RayGlutamate-tRNA LigaseModels, MolecularNitrogenous Group TransferasesProtein BindingProtein BiosynthesisRNA, Transfer, Amino AcylGlutamate-tRNA Ligaseglutamyl-tRNA(Gln)glutamyl-tRNA(Gln) amidotransferaseNitrogenous Group TransferasesRNA, Transfer, Amino Acyl

Identifiers

PMID21726564
PMCPMC3156345
OpenAlexW2046129745

What OpenQuestion holds

Textmetadata
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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.