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_36
Snippet: Because IFIT2 and IFIT3 were enriched to a similar degree in our IFIT1 pull down SILAC experiments we hypothesised that IFIT1 interacts with a heterodimer of IFIT2 and IFIT3. We therefore next examined if IFIT2 and IFIT3 could interact. Equal amounts of IFIT2 and IFIT3 were mixed and incubated at 4 ï‚°C for 1 hour. When analysed by SEC-MALS two peaks corresponding to IFIT2 and IFIT3 homodimers were clearly separated ( Figure 2B , grey dotted line.....
Document: Because IFIT2 and IFIT3 were enriched to a similar degree in our IFIT1 pull down SILAC experiments we hypothesised that IFIT1 interacts with a heterodimer of IFIT2 and IFIT3. We therefore next examined if IFIT2 and IFIT3 could interact. Equal amounts of IFIT2 and IFIT3 were mixed and incubated at 4 ï‚°C for 1 hour. When analysed by SEC-MALS two peaks corresponding to IFIT2 and IFIT3 homodimers were clearly separated ( Figure 2B , grey dotted line). In contrast, when IFIT2 and IFIT3 were instead incubated at 37 ï‚°C for 1 hour an IFIT2:IFIT3 heterodimer was formed ( Figure 2B , black dashed line). The molecular weight of the eluting species (110 kDa) and analysis by SDS-PAGE (gel inset) are consistent with this complex representing an IFIT2:IFIT3 heterodimer. To test the stability of the IFIT2:IFIT3 heterodimer, corresponding peak fractions were concentrated and author/funder. All rights reserved. No reuse allowed without permission.
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