Evidence map›Paper›PMID 27124620›Full record

ArticleProtein science : a publication of the Protein Society2016

Metal binding affinity and structural properties of calmodulin-like protein 14 from Arabidopsis thaliana.

Rosario Vallone, Valentina La Verde, Mariapina D'Onofrio, Alejandro Giorgetti, Paola Dominici, Alessandra Astegno

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
8.2field-weighted citation impact, top 4% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

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  14. Preferential Binding of MgFrontiers in molecular neuroscience · 2018
    Article
  15. The Journal of biological chemistry · 2017
    Article
  16. Article
  17. Frontiers in plant science · 2017
    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 1 institution in 1 country.

Rosario ValloneDepartment of Biotechnology, University of Verona, Verona, Italy.
Valentina La VerdeDepartment of Biotechnology, University of Verona, Verona, Italy.
Mariapina D'OnofrioDepartment of Biotechnology, University of Verona, Verona, Italy.
Alejandro GiorgettiDepartment of Biotechnology, University of Verona, Verona, Italy.
Paola DominiciDepartment of Biotechnology, University of Verona, Verona, Italy.
Alessandra AstegnoDepartment of Biotechnology, University of Verona, Verona, Italy.
University of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to the well-known Ca(2+) sensor calmodulin, plants possess many calmodulin-like proteins (CMLs) that are predicted to have specific roles in the cell. Herein, we described the biochemical and biophysical characterization of recombinant Arabidopsis thaliana CML14. We applied isothermal titration calorimetry to analyze the energetics of Ca(2+) and Mg(2+) binding to CML14, and nuclear magnetic resonance spectroscopy, together with intrinsic and ANS-based fluorescence, to evaluate the structural effects of metal binding and metal-induced conformational changes. Furthermore, differential scanning calorimetry and limited proteolysis were used to characterize protein thermal and local stability. Our data demonstrate that CML14 binds one Ca(2+) ion with micromolar affinity (Kd ∼ 12 µM) and the presence of 10 mM Mg(2+) decreases the Ca(2+) affinity by ∼5-fold. Although binding of Ca(2+) to CML14 increases protein stability, it does not result in a more hydrophobic protein surface and does not induce the large conformational rearrangement typical of Ca(2+) sensors, but causes only localized structural changes in the unique functional EF-hand. Our data, together with a molecular modelling prediction, provide interesting insights into the biochemical properties of Arabidopsis CML14 and may be useful to direct additional studies aimed at understanding its physiological role.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCalciumCalmodulinCations, DivalentCloning, MolecularConserved SequenceEF Hand MotifsEscherichia coliGene ExpressionHydrophobic and Hydrophilic InteractionsMagnesiumModels, MolecularMutationArabidopsis ProteinsCalciumCalmodulinCations, DivalentMagnesiumRecombinant ProteinsArabidopsis thalianacalcium bindingcalmodulin-like proteinconformational changeEF-handprotein stability

Identifiers

PMID27124620
PMCPMC4972202
OpenAlexW2346654194

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.