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Identification of a novel receptor-like protein kinase that interacts ith a geminivirus nuclear shuttle protein

Tipo de material: TextoTextoSeries ; Virology, 318(1), p.24-31, 2004Trabajos contenidos:
  • Mariano, A.C
  • Andrade, M.O
  • Santos, A.A
  • Carolino, S.M.B
  • Oliveira, M.L
  • Baracat-Pereira, M.C
  • Brommonshenkel, S.H
  • Brommonshenkel, S.H
Tema(s): Recursos en línea: Resumen: Despite extensive studies in plant virus-host interactions, the molecular mechanisms of geminivirus movement and interactions with host components remain largely unknown. A tomato kinase protein and its soybean homolog were found to interact specifically with the nuclear shuttle protein (NSP)of Tomato golden mosaic virus (TGMV)and Tomato crinkle leaf yellows virus (TCrLYV)through yeast two-hybrid screening and in vitro protein binding assays. These proteins, designated LeNIK (Lycopersicon esculentum NSP-Interacting Kinase)and GmNIK (Glycine max NIK), belong to the LRR-RLK (leucine rich-repeat receptor-like kinase)family that is involved in plant developmental processes and/or resistance response. As such, NIK is structurally organized into characteristic domains, including a serine/threonine kinase domain with a nucleotide binding site at the C-terminal region, an internal transmembrane segment and leucine-rich repeats (LRR)at the Nterminal portion. The potential significance of the NSP-NIK interaction is discussed.
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Despite extensive studies in plant virus-host interactions, the molecular mechanisms of geminivirus movement and interactions with host components remain largely unknown. A tomato kinase protein and its soybean homolog were found to interact specifically with the nuclear shuttle protein (NSP)of Tomato golden mosaic virus (TGMV)and Tomato crinkle leaf yellows virus (TCrLYV)through yeast two-hybrid screening and in vitro protein binding assays. These proteins, designated LeNIK (Lycopersicon esculentum NSP-Interacting Kinase)and GmNIK (Glycine max NIK), belong to the LRR-RLK (leucine rich-repeat receptor-like kinase)family that is involved in plant developmental processes and/or resistance response. As such, NIK is structurally organized into characteristic domains, including a serine/threonine kinase domain with a nucleotide binding site at the C-terminal region, an internal transmembrane segment and leucine-rich repeats (LRR)at the Nterminal portion. The potential significance of the NSP-NIK interaction is discussed.

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