Evidence map›Paper›PMID 23497186›Full record

ArticleBMC plant biology2013

Homo-dimerization and ligand binding by the leucine-rich repeat domain at RHG1/RFS2 underlying resistance to two soybean pathogens.

Ahmed J Afzal, Ali Srour, Abhishek Goil, Sheeja Vasudaven, Tianyun Liu, Ram Samudrala, Navneet Dogra, Punit Kohli, Ayan Malakar, David A Lightfoot

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2013. 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
2.8field-weighted citation impact, top 9% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structure and Emerging Functions of LRCH Proteins in Leukocyte Biology.Frontiers in cell and developmental biology · 2020
    Review
  5. Article
  6. Article
  7. Integration of sudden death syndrome resistance loci in the soybean genome.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2018
    Review
  8. Article
  9. Review
  10. 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

10 authors at 2 institutions in 1 country.

Ahmed J AfzalDepartment of Molecular Biology, Microbiology and Biochemistry and Center for Excellence the Illinois Soybean Center, Southern Illinois University at Carbondale, IL 62901, USA. ga4082@siu.edu
Ali Srour
Abhishek Goil
Sheeja Vasudaven
Tianyun Liu
Ram Samudrala
Navneet Dogra
Punit Kohli
Ayan Malakar
David A Lightfoot
Southern Illinois University Carbondale · USUniversity of Washington · US

Funding

NOVEL PARADIGMS FOR DRUG DISCOVERY: COMPUTATIONAL MULTITARGET SCREENINGDP1LM011509 · NLM · UNIVERSITY OF WASHINGTON · PI SAMUDRALA, RAM · 2012 to 2014
$2.4M
NOVEL PARADIGMS FOR DRUG DISCOVERY: COMPUTATIONAL MULTITARGET SCREENINGDP1OD006779 · OD · UNIVERSITY OF WASHINGTON · PI SAMUDRALA, RAM · 2010 to 2011
$1.7M
NIH HHS DP1 OD006779NLM NIH HHS DP1 LM011509
6 · The paper itself

Abstract

backgroundThe protein encoded by GmRLK18-1 (Glyma_18_02680 on chromosome 18) was a receptor like kinase (RLK) encoded within the soybean (Glycine max L. Merr.) Rhg1/Rfs2 locus. The locus underlies resistance to the soybean cyst nematode (SCN) Heterodera glycines (I.) and causal agent of sudden death syndrome (SDS) Fusarium virguliforme (Aoki). Previously the leucine rich repeat (LRR) domain was expressed in Escherichia coli.

resultsThe aims here were to evaluate the LRRs ability to; homo-dimerize; bind larger proteins; and bind to small peptides. Western analysis suggested homo-dimers could form after protein extraction from roots. The purified LRR domain, from residue 131-485, was seen to form a mixture of monomers and homo-dimers in vitro. Cross-linking experiments in vitro showed the H274N region was close (<11.1 A) to the highly conserved cysteine residue C196 on the second homo-dimer subunit. Binding constants of 20-142 nM for peptides found in plant and nematode secretions were found. Effects on plant phenotypes including wilting, stem bending and resistance to infection by SCN were observed when roots were treated with 50 pM of the peptides. Far-Western analyses followed by MS showed methionine synthase and cyclophilin bound strongly to the LRR domain. A second LRR from GmRLK08-1 (Glyma_08_g11350) did not show these strong interactions.

conclusionsThe LRR domain of the GmRLK18-1 protein formed both a monomer and a homo-dimer. The LRR domain bound avidly to 4 different CLE peptides, a cyclophilin and a methionine synthase. The CLE peptides GmTGIF, GmCLE34, GmCLE3 and HgCLE were previously reported to be involved in root growth inhibition but here GmTGIF and HgCLE were shown to alter stem morphology and resistance to SCN. One of several models from homology and ab-initio modeling was partially validated by cross-linking. The effect of the 3 amino acid replacements present among RLK allotypes, A87V, Q115K and H274N were predicted to alter domain stability and function. Therefore, the LRR domain of GmRLK18-1 might underlie both root development and disease resistance in soybean and provide an avenue to develop new variants and ligands that might promote reduced losses to SCN.

Indexed as

AnimalsDimerizationDisease ResistanceFusariumGlycine maxNematodaPlant DiseasesPlant ProteinsPlant Proteins

Identifiers

PMID23497186
PMCPMC3626623
OpenAlexW2171727274

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.