Institute for Plant Genomics

Szeged, Hungary

Institute for Plant Genomics

Szeged, Hungary
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PubMed | CAS Fujian Institute of Research on the Structure of Matter, Institute for Plant Genomics and Texas College
Type: Journal Article | Journal: Angewandte Chemie (International ed. in English) | Year: 2016

Using the amber suppression approach, N


Indrasumunar A.,University of Queensland | Indrasumunar A.,Indonesian Center for Agricultural Biotechnology | Searle I.,University of Queensland | Searle I.,Australian National University | And 7 more authors.
Plant Journal | Year: 2011

Two allelic non-nodulating mutants, nod49 and rj1, were characterized using map-based cloning and candidate gene approaches, and genetic complementation. From our results we propose two highly related lipo-oligochitin LysM-type receptor kinase genes (GmNFR1α and GmNFR1β) as putative Nod factor receptor components in soybean. Both mutants contained frameshift mutations in GmNFR1α that would yield protein truncations. Both mutants contained a seemingly functional GmNFR1β homeologue, characterized by a 374-bp deletion in intron 6 and 20-100 times lower transcript levels than GmNFR1α, yet both mutants were unable to form nodules. Mutations in GmNFR1β within other genotypes had no defects in nodulation, showing that GmNFR1β was redundant. Transgenic overexpression of GmNFR1α, but not of GmNFR1β, increased nodule number per plant, plant nitrogen content and the ability to form nodules with restrictive, ultra-low Bradyrhizobium japonicum titres in transgenic roots of both nod49 and rj1. GmNFR1α overexpressing roots also formed nodules in nodulation-restrictive acid soil (pH 4.7). Our results show that: (i) NFR1α expression controls nodule number in soybean, and (ii) acid soil tolerance for nodulation and suppression of nodulation deficiency at low titre can be achieved by overexpression of GmNFR1α. © 2010 Blackwell Publishing Ltd.


Indrasumunar A.,University of Queensland | Kereszt A.,University of Queensland | Kereszt A.,Institute for Plant Genomics | Searle I.,University of Queensland | And 7 more authors.
Plant and Cell Physiology | Year: 2010

Chemically induced non-nodulating nod139 and nn5 mutants of soybean (Glycine max) show no visible symptoms in response to rhizobial inoculation. Both exhibit recessive Mendelian inheritance suggesting loss of function. By allele determination and genetic complementation in nod139 and nn5, two highly related lipo-oligochitin LysM-type receptor kinase genes in Glycine max were cloned; they are presumed to be the critical nodulation-inducing (Nod) factor receptor similar to those of Lotus japonicus, pea and Medicago truncatula. These duplicated receptor genes were called GmNFR5α and GmNFR5β. Nonsense mutations in GmNFR5α and GmNFR5β were genetically complemented by both wild-type GmNFR5α and GmNFR5β in transgenic roots, indicating that both genes are functional. Both genes lack introns. In cultivar Williams82 GmNFR5α is located in chromosome 11 and in tandem with GmLYK7 (a related LysM receptor kinase gene), while GmNFR5β is in tandem with GmLYK4 in homologous chromosome 1, suggesting ancient synteny and regional segmental duplication. Both genes are wild type in G. soja CPI100070 and Harosoy63; however, a non-functional NFR5β allele (NFR5β (*)) was discovered in parental lines Bragg and Williams, which harbored an identical 1,407 bp retroelement-type insertion. This retroelement (GmRE-1) and related sequences are located in several soybean genome positions. Paradoxically, putatively unrelated soybean cultivars shared the same insertion, suggesting a smaller than anticipated genetic base in this crop. GmNFR5α but not GmNFR5β (*) was expressed in inoculated and uninoculated tap and lateral root portions at about 1025 of GmATS1 (ATP synthase subunit 1), but not in trifoliate leaves and shoot tips.


Burian K.,University of Szeged | Endresz V.,University of Szeged | Deak J.,University of Szeged | Kormanyos Z.,University of Szeged | And 3 more authors.
Journal of Infectious Diseases | Year: 2010

Background. Interferon γ (IFN-γ) is the major cytokine involved in the elimination of Chlamydia infection. Despite its importance, the combined effect of Chlamydia infection and IFN-γ on the gene expression of murine epithelial cells has only partially been described. Methods. The DNA chip method was used to evaluate the impact of IFN-γ and both the human strain Chlamydia trachomatis L2 infection and the murine strain Chlamydia muridarum infection on the transcriptome of murine epithelial cells. Results. The gene expression analysis revealed that IFN-γ had an enhancing effect on both the up-regulation and down-regulation of the epithelial gene expression. The influenced gene functional classes included cytokine and chemokine expression, antigen presentation, apoptosis, and genes involved in basic metabolic processes such as fatty acid oxidation. We also detected the up-regulation of various genes that could be directly antichlamydial, such as members of the p47 GTPase family, inducible nitric oxide synthase, and monokine induced by IFN-γ (MIG). As a functional validation of DNA chip data, we measured the antichlamydial effect of MIG on the extracellular form of Chlamydia. Conclusions. Our results show that IFN-γ is a key cytokine that primes epithelial cells to activate adaptive and innate immunity and to express antichlamydial effector genes both intracellularly and extracellularly. © 2010 by the Infectious Diseases Society of America. All rights reserved.


Virok D.P.,Institute for Plant Genomics | Simon D.,University of Szeged | Bozso Z.,University of Szeged | Rajko R.,University of Szeged | And 7 more authors.
Journal of Proteome Research | Year: 2011

Oligomeric amyloid-β is currently of interest in amyloid-β mediated toxicity and the pathogenesis of Alzheimers disease. Mapping the amyloid-β interaction partners could help to discover novel pathways in disease pathogenesis. To discover the amyloid-β interaction partners, we applied a protein array with more than 8100 unique recombinantly expressed human proteins. We identified 324 proteins as potential interactors of oligomeric amyloid-β. The Gene Ontology functional analysis of these proteins showed that oligomeric amyloid-β bound to multiple proteins with diverse functions both from extra and intracellular localizations. This undiscriminating binding phenotype indicates that multiple protein interactions mediate the toxicity of the oligomeric amyloid-β. The most highly impacted cellular system was the protein translation machinery. Oligomeric amyloid-β could bind to altogether 24 proteins involved in translation initiation and elongation. The binding of amyloid-β to purified rat hippocampal ribosomes validated the protein array results. More importantly, in vitro translation assays showed that the oligomeric amyloid-β had a concentration dependent inhibitory activity on translation. Our results indicate that the inhibited protein synthesis is one of the pathways that can be involved in the amyloid-beta induced neurotoxicity. © 2011 American Chemical Society.


Balogh E.P.,University of Szeged | Faludi I.,University of Szeged | Virok D.P.,Institute for Plant Genomics | Endresz V.,University of Szeged | Burian K.,University of Szeged
International Journal of Medical Microbiology | Year: 2011

CXC chemokines that lack the ELR motif, including the monokine induced by IFN-γ (MIG/CXCL9), the IFN-induced protein of 10. kDa (IP-10/CXCL10), and the IFN-inducible T-cell α-chemoattractant (I-TAC/CXCL11), have been shown to mediate the generation of type 1 immune responses and to possess defensin-like bactericidal effects. This study revealed that the infection of mice with Chlamydophila pneumoniae via the intranasal route resulted in the local expression of MIG/CXCL9, IP-10/CXCL10, and I-TAC/CXCL11. The expression of IP-10/CXCL10 and I-TAC/CXCL11 mRNA peaked on day 4. On day 7, the expression of MIG/CXCL9 mRNA in the infected lungs was increased 156-fold relative to that in the uninfected mouse lungs. MIG/CXCL9 was also detected at a protein level from day 1, with the highest concentration in the supernatants of the infected lungs on day 7. The expression of IFN-γ displayed similar kinetics. C. pneumoniae and its inactivated form also induced the production of MIG/CXCL9 in mouse fibroblasts and in the murine macrophage cell line J774A in vitro. Cotreatment of the tissue cultures with C. pneumoniae and different quantities of IFN-γ resulted in strong increases in MIG/CXCL9 production. Recombinant MIG/CXCL9 exerted dose-dependent antibacterial activity against C. pneumoniae. Significant antichlamydial activity of MIG/CXCL9 was observed after a 15-min incubation period. Chlamydial proteins at a molecular weight of 60. kDa were identified by Far-Western blot assay and liquid chromatography-tandem mass spectrometry as binding molecules of MIG/CXCL9. The results of these experiments suggest that MIG/CXCL9 might play an important role in the innate and acquired defense mechanisms against C. pneumoniae. © 2010 Elsevier GmbH.


PubMed | Institute for Plant Genomics
Type: Journal Article | Journal: Journal of proteome research | Year: 2011

Oligomeric amyloid- is currently of interest in amyloid- mediated toxicity and the pathogenesis of Alzheimers disease. Mapping the amyloid- interaction partners could help to discover novel pathways in disease pathogenesis. To discover the amyloid- interaction partners, we applied a protein array with more than 8100 unique recombinantly expressed human proteins. We identified 324 proteins as potential interactors of oligomeric amyloid-. The Gene Ontology functional analysis of these proteins showed that oligomeric amyloid- bound to multiple proteins with diverse functions both from extra and intracellular localizations. This undiscriminating binding phenotype indicates that multiple protein interactions mediate the toxicity of the oligomeric amyloid-. The most highly impacted cellular system was the protein translation machinery. Oligomeric amyloid- could bind to altogether 24 proteins involved in translation initiation and elongation. The binding of amyloid- to purified rat hippocampal ribosomes validated the protein array results. More importantly, in vitro translation assays showed that the oligomeric amyloid- had a concentration dependent inhibitory activity on translation. Our results indicate that the inhibited protein synthesis is one of the pathways that can be involved in the amyloid-beta induced neurotoxicity.

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