The prototype foamy virus integrase contains a potent but non-transferable nuclear localization signal in its C-terminal domain, with five critical arginine and lysine residues.
The study identifies the specific amino acid residues critical for the nuclear localization signal function of the prototype foamy virus integrase.
To analyse the potential karyophilic activity of prototype foamy viruses (PFVs), we expressed the PFV integrase (IN) and its mutants as fusion proteins with enhanced green fluorescence protein. The subcellular localization of the fusion proteins was investigated by fluorescence microscopy. The PFV IN was found to be karyophilic and targeted the fusion protein to the nucleus. Mutational analyses demonstrated that the PFV IN contains a potent but non-transferable nuclear localization signal (NLS) in its C-terminal domain and contains five arginine and lysine residues between amino acids 308 and 329 that are critical for its NLS function.
An et al. (2008) studied this question. Prototype foamy virus (PFV) integrase and its mutants was evaluated on Subcellular localization of the fusion proteins. The prototype foamy virus integrase contains a potent but non-transferable nuclear localization signal in its C-terminal domain, with five critical arginine and lysine residues.