Evidence map›Paper›PMID 27474115›Full record

ArticlePlant physiology2016

Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress.

Fionn McLoughlin, Eman Basha, Mary E Fowler, Minsoo Kim, Juliana Bordowitz, Surekha Katiyar-Agarwal, Elizabeth Vierling

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

82 citing papers in PubMed, 143 citations in OpenAlex.

  1. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
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  6. Molecular Insights into the Role ofPlants (Basel, Switzerland) · 2026
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  9. Heterologous WatermelonCurrent issues in molecular biology · 2025
    Article
  10. Review
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  13. Article
  14. Article
  15. Article
  16. Article
  17. Establishment and Maintenance of Heat-Stress Memory in Plants.International journal of molecular sciences · 2024
    Review
  18. Article
  19. Heat shock proteinPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  20. Review

22 more citing papers are in PubMed but not listed here.

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 2 countries.

Fionn McLoughlinBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).ORCID 0000-0002-2430-5074
Eman BashaBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).
Mary E FowlerBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).
Minsoo KimBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).
Juliana BordowitzBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).
Surekha Katiyar-AgarwalBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.).
Elizabeth VierlingBiochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003 (F.M., M.E.F., M.K., E.V.);Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 (E.B., M.K., J.B., S.K.-A.); andDepartment of Botany, Tanta University, Tanta 31527, Egypt (E.B.) vierling@biochem.umass.edu.ORCID 0000-0002-0066-4881
University of Arizona · USUniversity of Massachusetts Amherst · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitous small heat shock proteins (sHSPs) are well documented to act in vitro as molecular chaperones to prevent the irreversible aggregation of heat-sensitive proteins. However, the in vivo activities of sHSPs remain unclear. To investigate the two most abundant classes of plant cytosolic sHSPs (class I [CI] and class II [CII]), RNA interference (RNAi) and overexpression lines were created in Arabidopsis (Arabidopsis thaliana) and shown to have reduced and enhanced tolerance, respectively, to extreme heat stress. Affinity purification of CI and CII sHSPs from heat-stressed seedlings recovered eukaryotic translation elongation factor (eEF) 1B (α-, β-, and γ-subunits) and eukaryotic translation initiation factor 4A (three isoforms), although the association with CI sHSPs was stronger and additional proteins involved in translation were recovered with CI sHSPs. eEF1B subunits became partially insoluble during heat stress and, in the CI and CII RNAi lines, showed reduced recovery to the soluble cell fraction after heat stress, which was also dependent on HSP101. Furthermore, after heat stress, CI sHSPs showed increased retention in the insoluble fraction in the CII RNAi line and vice versa. Immunolocalization revealed that both CI and CII sHSPs were present in cytosolic foci, some of which colocalized with HSP101 and with eEF1Bγ and eEF1Bβ. Thus, CI and CII sHSPs have both unique and overlapping functions and act either directly or indirectly to protect specific translation factors in cytosolic stress granules.

Indexed as

Hot TemperatureArabidopsisElectrophoresis, Gel, Two-DimensionalEukaryotic Initiation Factor-4AGene Expression Regulation, PlantHeat-Shock Proteins, SmallImmunoblottingPeptide Elongation FactorsPlant ProteinsPlants, Genetically ModifiedProtein BindingProtein IsoformsProtein SubunitsRNA InterferenceSeedlingsStress, PhysiologicalEukaryotic Initiation Factor-4AHeat-Shock Proteins, SmallHSP101 protein, plantPeptide Elongation FactorsPlant ProteinsProtein IsoformsProtein SubunitsTranscription Factors

Identifiers

PMID27474115
PMCPMC5047077
OpenAlexW2528568605

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.