Skip to main content
. 2010 Nov 11;6(11):e1001186. doi: 10.1371/journal.ppat.1001186

Figure 5. Dual functions of critical residue K258 in regulating NiV-M nuclear-cytoplasmic trafficking.

Figure 5

(A) The matrix protein sequences of twelve viruses from different genera within the family Paramyxoviridae were aligned using CLUSTAL W (version 1.83). Positively charged amino acid residues that conform to the consensus for bipartite NLSs are colored green. The red arrow points to the lysine residue conserved among all twelve viruses. (B) K258 in NiV-M was mutated to alanine or arginine using site-directed mutagenesis. As control, K263, a non-conserved lysine in the vicinity of K258, was also mutated to arginine. HeLa cells transfected with the indicated constructs were stained with mouse anti-FLAG antibody and DAPI. K258A was excluded from the nucleus, whereas K258R was concentrated in the nucleus. The localization of K263R was similar to wild-type M. Quantification of cytoplasmic/nuclear fluorescence intensity ratios is shown in (C).