Evidence map›Paper›PMID 24694827›Full record

ArticleAnnals of botany2014

Molecular and ultrastructural analysis of forisome subunits reveals the principles of forisome assembly.

Boje Müller, Sira Groscurth, Matthias Menzel, Boris A Rüping, Richard M Twyman, Dirk Prüfer, Gundula A Noll

Open access · bronzeAbstract read
In one paragraph

Article in Annals of botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.5field-weighted citation impact, top 5% 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

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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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. The CaProtein science : a publication of the Protein Society · 2022
    Article
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  3. Non-model model organisms.BMC biology · 2017
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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

7 authors at 4 institutions in 2 countries.

Boje MüllerInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 8, 48143 Münster, Germany.
Sira GroscurthFraunhofer Institute for Molecular Biology and Applied Ecology IME, Schlossplatz 8, 48143 Münster, Germany.
Matthias MenzelFraunhofer Institute for Mechanics and Materials IWM, Walter-Hülse-Strasse 1, 06120 Halle, Germany.
Boris A RüpingInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 8, 48143 Münster, Germany.
Richard M TwymanTRM Ltd, PO Box 93, York YO43 3WE, UK.
Dirk PrüferInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 8, 48143 Münster, Germany Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Schlossplatz 8, 48143 Münster, Germany dpruefer@uni-muenster.de.
Gundula A NollInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 8, 48143 Münster, Germany.
University of Münster · DEFraunhofer Institute for Molecular Biology and Applied Ecology · DEFraunhofer Society · DETRM (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BACKGROUND AND

aimsForisomes are specialized structural phloem proteins that mediate sieve element occlusion after wounding exclusively in papilionoid legumes, but most studies of forisome structure and function have focused on the Old World clade rather than the early lineages. A comprehensive phylogenetic, molecular, structural and functional analysis of forisomes from species covering a broad spectrum of the papilionoid legumes was therefore carried out, including the first analysis of Dipteryx panamensis forisomes, representing the earliest branch of the Papilionoideae lineage. The aim was to study the molecular, structural and functional conservation among forisomes from different tribes and to establish the roles of individual forisome subunits.

methodsSequence analysis and bioinformatics were combined with structural and functional analysis of native forisomes and artificial forisome-like protein bodies, the latter produced by expressing forisome genes from different legumes in a heterologous background. The structure of these bodies was analysed using a combination of confocal laser scanning microscopy (CLSM), scanning electron microscopy (SEM) and transmission electron microscopy (TEM), and the function of individual subunits was examined by combinatorial expression, micromanipulation and light microscopy. KEY

resultsDipteryx panamensis native forisomes and homomeric protein bodies assembled from the single sieve element occlusion by forisome (SEO-F) subunit identified in this species were structurally and functionally similar to forisomes from the Old World clade. In contrast, homomeric protein bodies assembled from individual SEO-F subunits from Old World species yielded artificial forisomes differing in proportion to their native counterparts, suggesting that multiple SEO-F proteins are required for forisome assembly in these plants. Structural differences between Medicago truncatula native forisomes, homomeric protein bodies and heteromeric bodies containing all possible subunit combinations suggested that combinations of SEO-F proteins may fine-tune the geometric proportions and reactivity of forisomes.

conclusionsIt is concluded that forisome structure and function have been strongly conserved during evolution and that species-dependent subsets of SEO-F proteins may have evolved to fine-tune the structure of native forisomes.

Indexed as

Amino Acid SequenceComputational BiologyFabaceaeMicroscopy, ConfocalMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMolecular Sequence DataPhylogenyPlant ProteinsSequence AlignmentPlant ProteinsCanavalia gladiataDipteryx panamensisFabaceaeForisome evolutionLotus japonicusmacromolecular assemblyMedicago truncatulaPapilionoideaepapilionoid legumesPisum sativumSEOsieve element occlusion gene familystructural phloem proteinVicia faba

Identifiers

PMID24694827
PMCPMC4030808
OpenAlexW2149872372

What OpenQuestion holds

Textmetadata
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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.