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In orthotospovirus, the nonstructural NSs protein is the RNA silencing suppressor (RSS) and pathogenicity determinant. Here, we demonstrate that a putative α-helix, designated H8, spanning aa 338-369 of the C-terminal region of the NSs protein, is crucial for self-interaction of watermelon silver mottle virus (WSMoV) NSs protein and that the H8 affects RSS function. Co-immunoprecipitation, yeast two-hybrid and bimolecular fluorescence complementation analyses revealed that the triple point mutation (TPM) of H8 amino acids Y338A, H350A and F353A resulted in NSs protein self-interaction dysfunction. Transient expression of H8-deleted (ΔH8) and TPM NSs proteins in Nicotiana benthamiana plants by agroinfitration indicated that these proteins have weaker RSS activity and far less stable than wild type (WT) NSs. However, electrophoretic mobility assay revealed that siRNA binding ability of TPM NSs protein is not compromised. The pathogenicity assay of WT NSs protein expressed by the attenuated turnip mosaic virus (TuMV) vector restored severe symptoms in recombinant-infected N. benthamiana plants, but not for ΔH8 or TPM proteins. Taken together, we conclude that the H8 in the C-terminal region of NSs protein is crucial for stabilizing NSs protein through self-interaction to maintain normal functions of RSS and pathogenicity, but not for NSs-siRNA binding activity.
This article was published in the following journal.
Name: Molecular plant-microbe interactions : MPMI
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A family of DNA binding proteins that regulate expression of a variety of GENES during CELL DIFFERENTIATION and APOPTOSIS. Family members contain a highly conserved carboxy-terminal basic HELIX-TURN-HELIX MOTIF involved in dimerization and sequence-specific DNA binding.
A genomic region found in DROSOPHILA. The region contains genes encoding BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTORS that play a critical role in the regulation of pattern formation during EMBRYONIC DEVELOPMENT.
A family of eukaryotic transcription factors that recognize and bind to a highly-conserved cis-regulatory sequence (X-box) within the promoter region of MHC CLASS II GENES. They contain a conserved winged-helix DNA binding domain and function as homo or heterodimers.
Antimicrobial peptides that form channels in membranes that are more permeable to anions than cations. They resemble MAGAININS, with their N-terminal region forming a positively charged amphipathic alpha helix, but containing an additional C-terminal segment.
A family of vertebrate and insect lipid droplet associated proteins. They consist of a conserved N-terminal PAT domain (an alpha-helical region of about 110 amino acids), an 11-mer repeat region, and lipid-binding hydrophobic regions or 4-helix bundles near their C-termini. Perilipins transiently or constitutively localize to LIPID DROPLETS in ADIPOCYTES and FOAM CELLS, especially in regions adjacent to the PLASMA MEMBRANE and ENDOPLASMIC RECTICULUM. They are critical for lipid droplet synthesis and homeostasis as well as the regulation of lipid metabolism. Genetic variations in perilipins are associated with ATHEROSCLEROSIS; OBESITY; and DIABETES MELLITUS.
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