Characterization of the transport signals that mediate the nucleocytoplasmic traffic of low risk HPV11 E7

详细信息    查看全文

• 作者：Courtney H. McKee ; Zeynep Onder ; Aditya Ashok ; Rebeca Cardoso ; Junona Moroianu
• 关键词：HPV ; human papillomavirus ; NLS ; nuclear localization signal ; NES ; nuclear export signal ; EGFP ; enhanced green fluorescent protein ; GST ; glutathione-S-transferase
• 刊名：Virology
• 出版年：2013
• 出版时间：15 August, 2013
• 年：2013
• 卷：443
• 期：1
• 页码：113-122
• 全文大小：5653 K

文摘

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.