Fig. 2.

The interaction of CBC with NELF-E is enhanced in the presence of m⁷GTP. a Schematic diagram of the domain structure of NELF-E. b Gel filtration chromatogram and Coomassie-stained SDS-PAGE of CBC-NELF-E in the presence and absence of m⁷GTP. Purified recombinant CBC and NELF-E were mixed with (orange) or without (green) 500 µM m⁷GTP and subjected to gel filtration. Their elution profiles were overlaid (left) and single fractions analysed by SDS-PAGE (middle and right). Purified recombinant CBC and NELF-E^244–360 were mixed together with 500 µM m⁷GTP and similarly analysed (bottom left). c ITC data and curve fit to derive the affinity of different NELF-E constructs for CBC. CBC or m⁷GTP-CBC in the sample cell was titrated by NELF-E^244–380 or NELF-E^360–380. The data were presented as described in the caption to Fig. 1c. d Sequence alignment of the C-terminus of NELF-E. Conserved residues are highlighted in red. Figure made with ESPript⁵⁴