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_46
Snippet: The observation that many of the factors enriched using the VPg protein were only 481 enriched on complexes purified with NS1/2 tagged infectious MNV, could suggest 482 that the viral proteins present in the viral translation complex are distinct from those 483 present in complexes active for viral RNA synthesis. However, we cannot formally 484 rule out other possible explanations including the possibility that the specific 485 enrichment of tran.....
Document: The observation that many of the factors enriched using the VPg protein were only 481 enriched on complexes purified with NS1/2 tagged infectious MNV, could suggest 482 that the viral proteins present in the viral translation complex are distinct from those 483 present in complexes active for viral RNA synthesis. However, we cannot formally 484 rule out other possible explanations including the possibility that the specific 485 enrichment of translation factors on NS1/2 occurs because NS1/2 is the first protein 486 to be translated from ORF1, therefore unprocessed NS1/2 at the N-terminus of the 487 ORF1 polyprotein being actively translated could function as an anchor, facilitating 488 the enrichment of ribosomes and the associated factors. In addition, we have 489 previously seen that VPg-containing precursors may bind the translation initiation 490 factor eIF4G less well (Leen et al., 2016) , which could prevent some VPg (NS5) 491 containing precursors associating with translation initiation complexes. 492
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