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  • 1
    Publication Date: 2015-02-25
    Description: Plants and plant pathogens are subject to continuous co-evolutionary pressure for dominance, and the outcomes of these interactions can substantially impact agriculture and food security. In virus-plant interactions, one of the major mechanisms for plant antiviral immunity relies on RNA silencing, which is often suppressed by co-evolving virus suppressors, thus enhancing viral pathogenicity in susceptible hosts. In addition, plants use the nucleotide-binding and leucine-rich repeat (NB-LRR) domain-containing resistance proteins, which recognize viral effectors to activate effector-triggered immunity in a defence mechanism similar to that employed in non-viral infections. Unlike most eukaryotic organisms, plants are not known to activate mechanisms of host global translation suppression to fight viruses. Here we demonstrate in Arabidopsis that the constitutive activation of NIK1, a leucine-rich repeat receptor-like kinase (LRR-RLK) identified as a virulence target of the begomovirus nuclear shuttle protein (NSP), leads to global translation suppression and translocation of the downstream component RPL10 to the nucleus, where it interacts with a newly identified MYB-like protein, L10-INTERACTING MYB DOMAIN-CONTAINING PROTEIN (LIMYB), to downregulate translational machinery genes fully. LIMYB overexpression represses ribosomal protein genes at the transcriptional level, resulting in protein synthesis inhibition, decreased viral messenger RNA association with polysome fractions and enhanced tolerance to begomovirus. By contrast, the loss of LIMYB function releases the repression of translation-related genes and increases susceptibility to virus infection. Therefore, LIMYB links immune receptor LRR-RLK activation to global translation suppression as an antiviral immunity strategy in plants.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4779052/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4779052/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zorzatto, Cristiane -- Machado, Joao Paulo B -- Lopes, Kenia V G -- Nascimento, Kelly J T -- Pereira, Welison A -- Brustolini, Otavio J B -- Reis, Pedro A B -- Calil, Iara P -- Deguchi, Michihito -- Sachetto-Martins, Gilberto -- Gouveia, Bianca C -- Loriato, Virgilio A P -- Silva, Marcos A C -- Silva, Fabyano F -- Santos, Anesia A -- Chory, Joanne -- Fontes, Elizabeth P B -- 5R01-GM94428/GM/NIGMS NIH HHS/ -- R01 GM094428/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2015 Apr 30;520(7549):679-82. doi: 10.1038/nature14171. Epub 2015 Feb 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Departamento de Bioquimica e Biologia Molecular, National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil [2] National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil. ; 1] National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil [2] Departamento de Genetica, Universidade Federal do Rio de Janeiro, 21944.970 Rio de Janeiro, Brazil. ; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil. ; Departamento de Zootecnia, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil. ; 1] National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Vicosa, 36570.000 Vicosa, Minas Gerais, Brazil [2] Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25707794" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Arabidopsis/*immunology/*virology ; Arabidopsis Proteins/*metabolism ; Begomovirus/*immunology ; Cell Nucleus/metabolism ; Down-Regulation ; Gene Expression Regulation, Plant ; Immune Tolerance ; *Immunity, Innate ; *Plant Immunity ; Protein Binding ; Protein Biosynthesis/genetics/*immunology ; Protein-Serine-Threonine Kinases/*metabolism ; Ribosomal Proteins/metabolism ; Transcription Factors/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
  • 3
    Publication Date: 2013-11-27
    Description: Prolonged endoplasmic reticulum and osmotic stress synergistically activate the stress-induced N-rich protein-mediated signaling that transduces a cell death signal by inducing GmNAC81 (GmNAC6) in soybean. To identify novel regulators of the stress-induced programmed cell death (PCD) response, we screened a two-hybrid library for partners of GmNAC81. We discovered another member...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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