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Provedor de dados:  Genet. Mol. Biol.
País:  Brazil
Título:  Translational control in plant antiviral immunity
Autores:  Machado,João Paulo B.
Calil,Iara P.
Santos,Anésia A.
Fontes,Elizabeth P.B.
Data:  2017-01-01
Ano:  2017
Palavras-chave:  Translation suppression
Recessive resistance genes
Argonaute
NSP-Interacting Kinase
NIK
Resumo:  Abstract Due to the limited coding capacity of viral genomes, plant viruses depend extensively on the host cell machinery to support the viral life cycle and, thereby, interact with a large number of host proteins during infection. Within this context, as plant viruses do not harbor translation-required components, they have developed several strategies to subvert the host protein synthesis machinery to produce rapidly and efficiently the viral proteins. As a countermeasure against infection, plants have evolved defense mechanisms that impair viral infections. Among them, the host-mediated translational suppression has been characterized as an efficient mean to restrict infection. To specifically suppress translation of viral mRNAs, plants can deploy susceptible recessive resistance genes, which encode translation initiation factors from the eIF4E and eIF4G family and are required for viral mRNA translation and multiplication. Additionally, recent evidence has demonstrated that, alternatively to the cleavage of viral RNA targets, host cells can suppress viral protein translation to silence viral RNA. Finally, a novel strategy of plant antiviral defense based on suppression of host global translation, which is mediated by the transmembrane immune receptor NIK1 (nuclear shuttle protein (NSP)-Interacting Kinase1), is discussed in this review.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572017000200292
Editor:  Sociedade Brasileira de Genética
Relação:  10.1590/1678-4685-gmb-2016-0092
Formato:  text/html
Fonte:  Genetics and Molecular Biology v.40 n.1 suppl.1 2017
Direitos:  info:eu-repo/semantics/openAccess
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