Evidence map›Paper›PMID 15020769›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

A nascent polypeptide domain that can regulate translation elongation.

Peng Fang, Christina C Spevak, Cheng Wu, Matthew S Sachs

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.2field-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

43 citing papers in PubMed, 86 citations in OpenAlex.

  1. Tiny but mighty: Diverse functions of uORFs that regulate gene expression.Computational and structural biotechnology journal · 2024
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  19. Sequence selectivity of macrolide-induced translational attenuation.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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

4 authors at 1 institution in 1 country.

Peng FangDepartment of Environmental and Biomolecular Systems, OGI School of Science & Engineering, Oregon Health & Science University, Beaverton, OR 97006-8921, USA.
Christina C Spevak
Cheng Wu
Matthew S Sachs
Oregon Health & Science University · US

Funding

CONTROL OF ARG-2 GENE EXPRESSION IN NEUROSPORAR01GM047498 · NIGMS · TEXAS A&M UNIVERSITY · PI SACHS, MATTHEW STEVEN · 1997 to 2009
$2.8M
CONTROL OF ARG-2 GENE EXPRESSION IN NEUROSPORAR29GM047498 · NIGMS · OREGON GRADUATE INSTITUTE SCIENCE &TECH · PI SACHS, MATTHEW S · 1992 to 1996
–
NIGMS NIH HHS GM 47498NIGMS NIH HHS GM 47498-SNIGMS NIH HHS R01 GM047498
6 · The paper itself

Abstract

The evolutionarily conserved fungal arginine attenuator peptide (AAP), as a nascent peptide, stalls the translating ribosome in response to the presence of a high concentration of the amino acid arginine. Here we examine whether the AAP maintains regulatory function in fungal, plant, and animal cell-free translation systems when placed as a domain near the N terminus or internally within a large polypeptide. Pulse-chase analyses of the radiolabeled polypeptides synthesized in these systems indicated that wild-type AAP functions at either position to stall polypeptide synthesis in response to arginine. Toeprint analyses performed to map the positions of stalled ribosomes on transcripts introduced into the fungal system revealed that ribosome stalling required translation of the AAP coding sequence. The positions of the stalled ribosomes were consistent with the sizes of the radiolabeled polypeptide intermediates. These findings demonstrate that an internal polypeptide domain in a nascent chain can regulate eukaryotic translational elongation in response to a small molecule. Apparently the peptide-sensing features are conserved in fungal, plant, and animal ribosomes. These data provide precedents for translational strategies that would allow domains within nascent polypeptide chains to modulate gene expression.

Indexed as

Gene Expression RegulationProtein BiosynthesisCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorCetrimoniumCetrimonium CompoundsFungal ProteinsPeptide FragmentsProtein Structure, TertiaryTime Factorsarginine attenuator peptideCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorCetrimoniumCetrimonium CompoundsFungal ProteinsPeptide Fragments

Identifiers

PMID15020769
PMCPMC384695
OpenAlexW2019014293

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.