Selected article for: "complex form and presence absence"
Author: Myra Hosmillo; Jia Lu; Michael R. McAllaster; James B. Eaglesham; Xinjie Wang; Edward Emmott; Patricia Domingues; Yasmin Chaudhry; Timothy J Fitzmaurice; Matthew K.H. Tung; Marc Panas; Gerald McInerney; Nicholas Locker; Craig B. Willen; Ian Goodfellow
Title: Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation
  • Document date: 2019_3_8
    • ID: d0q5lhf4_27
    Snippet: Our proteomics analysis also confirms that the norovirus VPg proteins form a 309 complex that contains multiple components of the 40S subunit ( Fig 1D) and it has 310 been established previously that G3BP1 associates with 40S subunits (Kedersha et 311 al., 2016) . To assess a potential role for G3BP1 in the formation of VPg-driven 312 translation complexes in cells, we examined the ability of GFP tagged version of 313 MNV VPg to pull down 40S sub.....
    Document: Our proteomics analysis also confirms that the norovirus VPg proteins form a 309 complex that contains multiple components of the 40S subunit ( Fig 1D) and it has 310 been established previously that G3BP1 associates with 40S subunits (Kedersha et 311 al., 2016) . To assess a potential role for G3BP1 in the formation of VPg-driven 312 translation complexes in cells, we examined the ability of GFP tagged version of 313 MNV VPg to pull down 40S subunits in the presence and absence of G3BP1. GFP-314 tagged WT MNV VPg was readily able to pull down eIF4G, G3BP1 and RpS6, a 315 component of the 40S subunit ( Fig 9A) . However, in the absence of G3BP1, the 316 ability to pull down RpS6 was lost ( Fig 9A) . Furthermore, we found that disruption of 317 the VPg-eIF4G interaction by the introduction of the F123A mutation into the eIF4G 318 binding domain, also significantly reduced the ability to pull down RpS6 (Fig 9B) . 319

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