Extended Data Fig. 10: FG pocket and capsid surface residues contribute different qualities of FG interactions.
From: Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition
Partitioning experiments into the GLFG 12mer FG phase of CLP mutations were performed as in Fig. 3, but the NaCl concentration was varied from 50 mM to 600 mM as indicated in panels a-e. Note that wildtype CLPs showed a perfect FG phase partitioning at all salt concentrations. N57A mutant CLPs showed a strong partitioning defect at 50 mM, 75 mM, 150 mM, and 250 mM NaCl; however, at 600 mM NaCl, the N57A mutant CLPs efficiently entered the FG phase. The A92E and G94D mutations showed a strong partitioning defect at any salt concentration. The Q9E mutant CLPs entered the phase at low salt, but showed a partitioning defect at higher salt. These different behaviors indicate that N57 and the critical surface residues mediate interactions of different qualities. Experiments were independently replicated two times with consistent outcomes.
