Evidence map›Paper›PMID 26442018›Full record

ArticleFrontiers in plant science2015

Nuclear localization of the dehydrin OpsDHN1 is determined by histidine-rich motif.

Itzell E Hernández-Sánchez, Israel Maruri-López, Alejandro Ferrando, Juan Carbonell, Steffen P Graether, Juan F Jiménez-Bremont

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.2field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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 3 institutions in 3 countries.

Itzell E Hernández-SánchezLaboratorio de Biología Molecular de Hongos y Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC San Luis Potosí, México.
Israel Maruri-LópezLaboratorio de Biología Molecular de Hongos y Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC San Luis Potosí, México.
Alejandro FerrandoInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas Valencia, Spain.
Juan CarbonellInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas Valencia, Spain.
Steffen P GraetherDepartment of Molecular and Cellular Biology, University of Guelph Guelph, ON, Canada.
Juan F Jiménez-BremontLaboratorio de Biología Molecular de Hongos y Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC San Luis Potosí, México.
Institute for Scientific and Technological Research · MXInstituto de Biología Molecular y Celular de Plantas · ESUniversity of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cactus OpsDHN1 dehydrin belongs to a large family of disordered and highly hydrophilic proteins known as Late Embryogenesis Abundant (LEA) proteins, which accumulate during the late stages of embryogenesis and in response to abiotic stresses. Herein, we present the in vivo OpsDHN1 subcellular localization by N-terminal GFP translational fusion; our results revealed a cytoplasmic and nuclear localization of the GFP::OpsDHN1 protein in Nicotiana benthamiana epidermal cells. In addition, dimer assembly of OpsDHN1 in planta using a Bimolecular Fluorescence Complementation (BiFC) approach was demonstrated. In order to understand the in vivo role of the histidine-rich motif, the OpsDHN1-ΔHis version was produced and assayed for its subcellular localization and dimer capability by GFP fusion and BiFC assays, respectively. We found that deletion of the OpsDHN1 histidine-rich motif restricted its localization to cytoplasm, but did not affect dimer formation. In addition, the deletion of the S-segment in the OpsDHN1 protein affected its nuclear localization. Our data suggest that the deletion of histidine-rich motif and S-segment show similar effects, preventing OpsDHN1 from getting into the nucleus. Based on these results, the histidine-rich motif is proposed as a targeting element for OpsDHN1 nuclear localization.

Indexed as

BiFCdehydrinhistidine-rich motifhomodimernuclear/cytoplasmic localization

Identifiers

PMID26442018
PMCPMC4561349
OpenAlexW1861724253

What OpenQuestion 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 OpenQuestion graph.