Evidence map›Paper›PMID 17483287›Full record

ArticleEukaryotic cell2007

Protein arginine methylation in Candida albicans: role in nuclear transport.

Anne E McBride, Cecilia Zurita-Lopez, Anthony Regis, Emily Blum, Ana Conboy, Shannon Elf, Steven Clarke

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. The MethyltransferaseJournal of fungi (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Review
  4. Multi-Omics Profiling ofMicroorganisms · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Cellular consequences of arginine methylation.Cellular and molecular life sciences : CMLS · 2019
    Review
  9. Article
  10. TheFrontiers in cellular and infection microbiology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  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

7 authors at 2 institutions in 1 country.

Anne E McBrideDepartment of Biology, 6500 College Station, Bowdoin College, Brunswick, ME 04011, USA. amcbride@bowdoin.edu
Cecilia Zurita-Lopez
Anthony Regis
Emily Blum
Ana Conboy
Shannon Elf
Steven Clarke
Bowdoin College · USUniversity of California, Los Angeles · US

Funding

CONTROL OF EUCARYOTIC FUNCTION BY METHYLATIONR37GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2009
$5.0M
CONTROL OF EUKARYOTIC MEMBRANE FUNCTION BY METHYLATIONR01GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 1985 to 2013
$2.1M
NIGMS NIH HHS GM026020NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R37 GM026020
6 · The paper itself

Abstract

Protein arginine methylation plays a key role in numerous eukaryotic processes, such as protein transport and signal transduction. In Candida albicans, two candidate protein arginine methyltransferases (PRMTs) have been identified from the genome sequencing project. Based on sequence comparison, C. albicans candidate PRMTs display similarity to Saccharomyces cerevisiae Hmt1 and Rmt2. Here we demonstrate functional homology of Hmt1 between C. albicans and S. cerevisiae: CaHmt1 supports growth of S. cerevisiae strains that require Hmt1, and CaHmt1 methylates Npl3, a major Hmt1 substrate, in S. cerevisiae. In C. albicans strains lacking CaHmt1, asymmetric dimethylarginine and omega-monomethylarginine levels are significantly decreased, indicating that Hmt1 is the major C. albicans type I PRMT1. Given the known effects of type I PRMTs on nuclear transport of RNA-binding proteins, we tested whether Hmt1 affects nuclear transport of a putative Npl3 ortholog in C. albicans. CaNpl3 allows partial growth of S. cerevisiae npl3Delta strains, but its arginine-glycine-rich C terminus can fully substitute for that of ScNpl3 and also directs methylation-sensitive association with ScNpl3. Expression of green fluorescent protein-tagged CaNpl3 proteins in C. albicans strains with and without CaHmt1 provides evidence for CaHmt1 facilitating export of CaNpl3 in this fungus. We have also identified the C. albicans Rmt2, a type IV fungus- and plant-specific PRMT, by amino acid analysis of an rmt2Delta/rmt2Delta strain, as well as biochemical evidence for additional cryptic PRMTs.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceArginineCandida albicansMethylationMolecular Sequence DataNuclear ProteinsProtein-Arginine N-MethyltransferasesRepressor ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSequence AlignmentArginineHMT1 protein, S cerevisiaeNPL3 protein, S cerevisiaeNuclear ProteinsProtein-Arginine N-MethyltransferasesRepressor ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17483287
PMCPMC1951101
OpenAlexW2101402793

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.