Evidence map›Paper›PMID 30047030›Full record

ArticleExtremophiles : life under extreme conditions2018

Modification of translation factor aIF5A from Sulfolobus solfataricus.

F Bassani, A Romagnoli, T Cacciamani, A Amici, D Benelli, P Londei, B Märtens, U Bläsi, A La Teana

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Extremophiles : life under extreme conditions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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 3 institutions in 2 countries.

F BassaniDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Via Brecce Bianche, 60131, Ancona, Italy.
A RomagnoliDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Via Brecce Bianche, 60131, Ancona, Italy.
T CacciamaniDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Via Brecce Bianche, 60131, Ancona, Italy.
A AmiciDepartment of Clinical Sciences, Section of Biochemistry, Polytechnic University of Marche, Via Ranieri 67, 60131, Ancona, Italy.
D BenelliDepartment of Cellular Biotechnologies and Haematology, Sapienza University of Rome, Via Regina Elena 324, 00161, Rome, Italy.
P LondeiDepartment of Cellular Biotechnologies and Haematology, Sapienza University of Rome, Via Regina Elena 324, 00161, Rome, Italy.
B MärtensDepartment of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, 1030, Vienna, Austria.
U BläsiDepartment of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, 1030, Vienna, Austria.
A La TeanaDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Via Brecce Bianche, 60131, Ancona, Italy. a.lateana@univpm.it.ORCID http://orcid.org/0000-0001-6232-0497
Marche Polytechnic University · ITSapienza University of Rome · ITUniversity of Vienna · AT

Funding

Austrian Science Fund 22888Polytechnic University of Marche RSA 2017
6 · The paper itself

Abstract

Eukaryotic eIF5A and its bacterial orthologue EF-P are translation elongation factors whose task is to rescue ribosomes from stalling during the synthesis of proteins bearing particular sequences such as polyproline stretches. Both proteins are characterized by unique post-translational modifications, hypusination and lysinylation, respectively, which are essential for their function. An orthologue is present in all Archaea but its function is poorly understood. Here, we show that aIF5A of the crenarchaeum Sulfolobus solfataricus is hypusinated and forms a stable complex with deoxyhypusine synthase, the first enzyme of the hypusination pathway. The recombinant enzyme is able to modify its substrate in vitro resulting in deoxyhypusinated aIF5A. Moreover, with the aim to identify the enzyme involved in the second modification step, i.e. hypusination, a set of proteins interacting with aIF5A was identified.

Indexed as

Protein Processing, Post-TranslationalArchaeal ProteinsLysinePeptide Initiation FactorsSulfolobus solfataricusArchaeal ProteinshypusineLysinePeptide Initiation FactorsDeoxyhypusine synthaseHypusinationPost-translational modificationSulfolobus solfataricusTranslation factor aIF5A

Identifiers

PMID30047030
PMCPMC6105217
OpenAlexW2883881082

What Socratic 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 Socratic graph.