AI Article Synopsis
- * A newly identified leucine-rich nuclear export signal (NES) within the zinc-binding domain helps facilitate the nuclear export of HPV11 E7 through a CRM1-dependent mechanism.
- * Hydrophobic interactions between a specific patch in the zinc-binding domain and FG-repeats of Nup62 are crucial for the nuclear import of HPV11 E7, with certain mutations disrupting this localization.
Article Abstract
We previously discovered that nuclear import of low risk HPV11 E7 is mediated by its zinc-binding domain via a pathway that is independent of karyopherins/importins (Piccioli et al., 2010. Virology 407, 100-109). In this study we mapped and characterized a leucine-rich nuclear export signal (NES), 76IRQLQDLLL84, within the zinc-binding domain that mediates the nuclear export of HPV11 E7 in a CRM1-dependent manner. We also identified a mostly hydrophobic patch 65VRLVV69 within the zinc-binding domain that mediates nuclear import of HPV11 E7 via hydrophobic interactions with the FG-repeats domain of Nup62. Substitutions of hydrophobic residues to alanine within the 65VRLVV69 sequence disrupt the nuclear localization of 11E7, whereas the R66A mutation has no effect. Overall the data support a model of nuclear entry of HPV11 E7 protein via hydrophobic interactions with FG nucleoporins at the nuclear pore complex.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3758764 | PMC |
| http://dx.doi.org/10.1016/j.virol.2013.04.031 | DOI Listing |
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