Evidence map›Paper›PMID 24999344›Full record

ArticleFrontiers in plant science2014

The selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes.

Hélène Hardré, Lauriane Kuhn, Catherine Albrieux, Juliette Jouhet, Morgane Michaud, Daphné Seigneurin-Berny, Denis Falconet, Maryse A Block, Eric Maréchal

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 45% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Hélène HardréLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Lauriane KuhnLaboratoire de Biologie à Grande Echelle, iRTSV CEA Grenoble, Grenoble, France.
Catherine AlbrieuxLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Juliette JouhetLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Morgane MichaudLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Daphné Seigneurin-BernyLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Denis FalconetLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Maryse A BlockLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Eric MaréchalLaboratoire de Physiologie Cellulaire et Végétale, UMR 5168 CNRS-CEA-INRA-Université Grenoble Alpes, iRTSV CEA Grenoble, Grenoble, France.
Université Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The understanding of chloroplast function requires the precise localization of proteins in each of its sub-compartments. High-sensitivity mass spectrometry has allowed the inventory of proteins in thylakoid, stroma, and envelope fractions. Concerning membrane association, proteins can be either integral or peripheral or even soluble proteins bound transiently to a membrane complex. We sought a method providing information at the surface of the outer envelope membrane (OEM), based on specific tagging with biotin or proteolysis using thermolysin, a non-membrane permeable protease. To evaluate this method, envelope, thylakoid, and stroma proteins were separated by two-dimensional electrophoresis and analyzed by immunostaining and mass spectrometry. A short selection of proteins associated to the chloroplast envelope fraction was checked after superficial treatments of intact chloroplasts. We showed that this method could allow the characterization of OEM embedded proteins facing the cytosol, as well as peripheral and soluble proteins associated via tight or lose interactions. Some stromal proteins were associated with biotinylated spots and analyzes are still needed to determine whether polypeptides were tagged prior import or if they co-migrated with OEM proteins. This method also suggests that some proteins associated with the inner envelope membrane (IEM) might need the integrity of a trans-envelope (IEM-OEM) protein complex (e.g., division ring-forming components) or at least an intact OEM partner. Following this evaluation, proteomic analyzes should be refined and the putative role of inter-membrane space components stabilizing trans-envelope complexes demonstrated. For future comprehensive studies, perspectives include the dynamic analyses of OEM proteins and IEM-OEM complexes in various physiological contexts and using virtually any other purified membrane organelle.

Indexed as

biotinylationchloroplast envelopemembrane protein complexesouter envelope proteinthermolysin

Identifiers

PMID24999344
PMCPMC4064156
OpenAlexW2099441198

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.