Evidence map›Paper›PMID 31403664›Full record

ArticleJournal of experimental botany2019

Barley cysteine protease PAP14 plays a role in degradation of chloroplast proteins.

Susann Frank, Julien Hollmann, Maria Mulisch, Andrea Matros, Cristian C Carrión, Hans-Peter Mock, Götz Hensel, Karin Krupinska

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

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  7. Identifying aPeerJ · 2024
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  11. Chloroplast dismantling in leaf senescence.Journal of experimental botany · 2021
    Review
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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

8 authors at 3 institutions in 2 countries.

Susann FrankInstitute of Botany, Christian-Albrechts-University of Kiel, Olshausenstraße 40, 24098 Kiel, Germany.
Julien HollmannInstitute of Botany, Christian-Albrechts-University of Kiel, Olshausenstraße 40, 24098 Kiel, Germany.
Maria MulischInstitute of Botany, Christian-Albrechts-University of Kiel, Olshausenstraße 40, 24098 Kiel, Germany.
Andrea MatrosLeibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstrasse 3, Seeland, OT Gatersleben, Germany.
Cristian C CarriónInstituto de Fisiología Vegetal, INFIVE, CONICET-UNLP, cc 327, 1900 La Plata, Argentina.
Hans-Peter MockLeibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstrasse 3, Seeland, OT Gatersleben, Germany.
Götz HenselLeibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstrasse 3, Seeland, OT Gatersleben, Germany.
Karin KrupinskaInstitute of Botany, Christian-Albrechts-University of Kiel, Olshausenstraße 40, 24098 Kiel, Germany.
Christian-Albrechts-Universität zu Kiel · DELeibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK) · DEConsejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast protein degradation is known to occur both inside chloroplasts and in the vacuole. Genes encoding cysteine proteases have been found to be highly expressed during leaf senescence. However, it remains unclear where they participate in chloroplast protein degradation. In this study HvPAP14, which belongs to the C1A family of cysteine proteases, was identified in senescing barley (Hordeum vulgare L.) leaves by affinity enrichment using the mechanism-based probe DCG-04 targeting cysteine proteases and subsequent mass spectrometry. Biochemical analyses and expression of a HvPAP14:RFP fusion construct in barley protoplasts was used to identify the subcellular localization and putative substrates of HvPAP14. The HvPAP14:RFP fusion protein was detected in the endoplasmic reticulum and in vesicular bodies. Immunological studies showed that HvPAP14 was mainly located in chloroplasts, where it was found in tight association with thylakoid membranes. The recombinant enzyme was activated by low pH, in accordance with the detection of HvPAP14 in the thylakoid lumen. Overexpression of HvPAP14 in barley revealed that the protease can cleave LHCB proteins and PSBO as well as the large subunit of Rubisco. HvPAP14 is involved in the normal turnover of chloroplast proteins and may have a function in bulk protein degradation during leaf senescence.

Indexed as

ProteolysisChloroplast ProteinsChloroplastsCysteine ProteasesEndoplasmic ReticulumHordeumHydrogen-Ion ConcentrationModels, BiologicalPlant LeavesPlants, Genetically ModifiedProtein TransportRecombinant ProteinsSubstrate SpecificityChloroplast ProteinsCysteine ProteasesRecombinant ProteinsBarleychloroplastcysteine proteaseHordeum vulgare LHvPAP14 (CAQ00109.1)leaf senescenceRubiscothylakoid membranes

Identifiers

PMID31403664
PMCPMC6859807
OpenAlexW2968640686

What OpenQuestion holds

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LicenceCC BY-NC
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.