Evidence map›Paper›PMID 20884617›Full record

ArticleThe Journal of biological chemistry2010

Sequence requirements for ribosome stalling by the arginine attenuator peptide.

Christina C Spevak, Ivaylo P Ivanov, Matthew S Sachs

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

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  11. Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018
    Review
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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

3 authors at 2 institutions in 2 countries.

Christina C SpevakDepartment of Neurobiology, The Scripps Research Institute, La Jolla, California 92037, USA.
Ivaylo P Ivanov
Matthew S Sachs
Texas A&M University · USUniversity College Cork · IE

Funding

CONTROL OF ARG-2 GENE EXPRESSION IN NEUROSPORAR01GM047498 · NIGMS · TEXAS A&M UNIVERSITY · PI SACHS, MATTHEW STEVEN · 1997 to 2009
$2.8M
NIGMS NIH HHS R01 GM047498NIGMS NIH HHS R01GM47498
6 · The paper itself

Abstract

The 5' regions of eukaryotic mRNAs often contain upstream open reading frames (uORFs). The Neurospora crassa arg-2 uORF encodes the 24-residue arginine attenuator peptide (AAP). This regulatory uORF-encoded peptide, which is evolutionarily conserved in fungal transcripts specifying an arginine biosynthetic enzyme, functions as a nascent peptide within the ribosomal tunnel and negatively regulates gene expression. The nascent AAP causes ribosomes to stall at the uORF stop codon in response to arginine, thus, blocking ribosomes from reaching the ARG-2 initiation codon. Here scanning mutagenesis with alanine and proline was performed to systematically determine which AAP residues were important for conferring regulation. Changing many of the most highly conserved residues (Asp-12, Tyr-13, Lys-14, and Trp-19) abolished regulatory function. The minimal functional domain of the AAP was determined by positioning AAP sequences internally within a large polypeptide. Pulse-chase analyses revealed that residues 9-20 of the AAP composed the minimal domain that was sufficient to confer regulatory function. An extensive analysis of predicted fungal AAPs revealed that the minimal functional domain of the N. crassa AAP corresponded closely to the region that was most highly conserved among the fungi. We also observed that the tripeptide RGD could function similarly to arginine in triggering AAP-mediated ribosome stalling. These studies provide a better understanding of the elements required for a nascent peptide and a small regulatory molecule to control translational processes.

Indexed as

Amino Acid SubstitutionCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorCodon, InitiatorFungal ProteinsMutation, MissenseNeurospora crassaPeptide FragmentsProtein BiosynthesisProtein Structure, TertiaryRibosomesRNA, Fungalarginine attenuator peptideCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorCodon, InitiatorFungal ProteinsPeptide FragmentsRNA, Fungal

Identifiers

PMID20884617
PMCPMC3003393
OpenAlexW2085803345

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.