Evidence map›Paper›PMID 9872948›Full record

ArticleGenetics1999

Saccharomyces cerevisiae Mod5p-II contains sequences antagonistic for nuclear and cytosolic locations.

L H Tolerico, A L Benko, J P Aris, D R Stanford, N C Martin, A K Hopper

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 55 citations in OpenAlex.

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  13. Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Review
  16. tRNA biology charges to the front.Genes & development · 2010
    Review
  17. Article
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  20. 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

6 authors at 4 institutions in 2 countries.

L H TolericoProgram in Cell and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, USA.
A L Benko
J P Aris
D R Stanford
N C Martin
A K Hopper
Institute of Molecular and Cell Biology · RUPennsylvania State University · USUniversity of Florida Health Science Center · USUniversity of Louisville · US

Funding

NUCLEOLAR FUNCTION AND CELL GROWTH IN YEASTR01GM048586 · NIGMS · UNIVERSITY OF FLORIDA · PI ARIS, JOHN P · 1994 to 1998
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NIGMS NIH HHS R01 GM048586
6 · The paper itself

Abstract

MOD5 encodes a tRNA modification activity located in three subcellular compartments. Alternative translation initiation generates Mod5p-I, located in the mitochondria and the cytosol, and Mod5p-II, located in the cytosol and nucleus. Here we study the nucleus/cytosol distribution of overexpressed Mod5p-II. Nuclear Mod5p-II appears concentrated in the nucleolus, perhaps indicating that the nuclear pool may have a different biological role than the cytoplasmic and mitochondrial pools. Mod5p contains three motifs resembling bipartite-like nuclear localization sequences (NLSs), but only one is sufficient to locate a passenger protein to the nucleus. Mutations of basic residues of this motif cumulatively contribute to a cytosolic location for the fusion proteins. These alterations also cause decreased nuclear pools of endogenous Mod5p-II. Depletion of nuclear Mod5p-II does not affect tRNATyr function. Despite the NLS, most Mod5p is cytosolic. We assessed whether Mod5p sequences cause a karyophilic reporter to be located in the cytosol. By this assay, Mod5p may contain more than one region that functions as cytoplasmic retention and/or nuclear export sequences. Thus, distribution of Mod5p results from the presence/absence of mitochondrial targeting information and sequences antagonistic for nuclear and cytosolic locations. Mod5p is highly conserved; sequences responsible for subcellular distribution appear to reside in "accessory" motifs missing from prokaryotic counterparts.

Indexed as

Alkyl and Aryl TransferasesSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBiological TransportCell NucleusCytoplasmCytosolHumansIsoenzymesMolecular Sequence DataNuclear Localization SignalsProteinsSaccharomyces cerevisiaeSubcellular FractionsAlkyl and Aryl TransferasesIsoenzymesMOD5 protein, S cerevisiaeNuclear Localization SignalsProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9872948
PMCPMC1460473
OpenAlexW2121303453

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.