Selected article for: "glycerol gradient and gradient sedimentation"
Author: Renata C Fleith; Harriet V Mears; Edward Emmott; Stephen C Graham; Daniel S Mansur; Trevor R Sweeney
Title: IFIT3 and IFIT2/3 promote IFIT1-mediated translation inhibition by enhancing binding to non-self RNA
  • Document date: 2018_2_8
    • ID: j97gul0w_5
    Snippet: An intriguing feature of IFITs is their propensity to homo and heterooligomerise. Using pull-down experiments of differentially tagged IFITs, Stawowczyk et al. (29) demonstrated that IFIT2 could interact both with itself and with IFIT1 and IFIT3 in HeLa cells. In the same study, an IFIT1, IFIT2 and IFIT3 containing complex in HeLa cytoplasmic lysates was also reported to migrate between 150-200 kDa when analysed by glycerol gradient sedimentation.....
    Document: An intriguing feature of IFITs is their propensity to homo and heterooligomerise. Using pull-down experiments of differentially tagged IFITs, Stawowczyk et al. (29) demonstrated that IFIT2 could interact both with itself and with IFIT1 and IFIT3 in HeLa cells. In the same study, an IFIT1, IFIT2 and IFIT3 containing complex in HeLa cytoplasmic lysates was also reported to migrate between 150-200 kDa when analysed by glycerol gradient sedimentation. Deletion analysis identified the first four TPRs of IFIT2 as being important for interaction with IFIT3 while the TPR(s) of IFIT2 that promote interaction with IFIT1 could not be elucidated (29) . IFIT1 was later reported to interact with IFIT2 or IFIT3 by size exclusion chromatography (SEC) (12) . The crystal structure of IFIT2 revealed it forms a stable, domain-swapped dimer, with TPRs of the N-terminal domain exchanged between each monomer (7) . Using native gel electrophoresis, we previously demonstrated IFIT1 and IFIT3 could homooligomerise (13) , while a recently-reported crystal structure of IFIT1 identified a motif in the C terminus responsible for IFIT1 dimerisation (BioRxiv: https://doi.org/10.1101/152850).

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