AI Article Synopsis

  • BCTV C4 protein interacts with two shaggy-related kinases (AtSKeta and AtSKzeta) and a putative LRR-RLK in a yeast two-hybrid assay, while TGMV AC4 only interacts with the kinases.
  • In vitro binding assays confirmed the interaction between BCTV C4 and AtSKeta, which also autophosphorylates and phosphorylates BCTV C4 at specific residues, though TGMV AC4 is phosphorylated less efficiently.
  • BCTV C4's localization at the cell membrane requires a specific N-terminal modification and certain amino acids affect its disease-causing ability, suggesting its role in influencing brassinosteroid signaling in plants.

Article Abstract

Beet curly top virus (BCTV) C4 interacted with two members of the shaggy-related protein kinase family (AtSKeta and AtSKzeta) and a putative leucine-rich repeat receptor-like kinase (LRR-RLK) in a yeast two-hybrid assay. Tomato golden mosaic virus (TGMV) AC4 also bound with similar efficiency to AtSKeta and AtSKzeta but was unable to interact with the LRR-RLK. BCTV C4 interaction with AtSKeta was confirmed using an in vitro binding assay. The protein kinases were capable of autophosphorylation in vitro and AtSKeta phosphorylated BCTV C4 at threonine and serine residues. AtSKeta phosphorylation of TGMV AC4 was significantly less efficient. The LRR-RLK did not efficiently phosphorylate BCTV C4. BCTV C4 localisation to the cell periphery in Nicotiana benthamiana was dependent on an intact N-terminal myristoylation motif, consistent with plasma membrane targeting. The intact motif was also required to produce the wild-type disease phenotype. Transient expression of BCTV C4 and TGMV AC4 derivatives in N. benthamiana identified additional amino acids within a central domain that contribute to the phenotype. The interaction with AtSKeta indicates that BCTV C4 interacts with the brassinosteroid signalling pathway.

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http://dx.doi.org/10.1016/j.virol.2006.12.034DOI Listing

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Article Synopsis
  • BCTV C4 protein interacts with two shaggy-related kinases (AtSKeta and AtSKzeta) and a putative LRR-RLK in a yeast two-hybrid assay, while TGMV AC4 only interacts with the kinases.
  • In vitro binding assays confirmed the interaction between BCTV C4 and AtSKeta, which also autophosphorylates and phosphorylates BCTV C4 at specific residues, though TGMV AC4 is phosphorylated less efficiently.
  • BCTV C4's localization at the cell membrane requires a specific N-terminal modification and certain amino acids affect its disease-causing ability, suggesting its role in influencing brassinosteroid signaling in plants.
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