人巨细胞病毒 pUL69 的 UAP56 相互作用基序转移到其鼠巨细胞病毒同源物中，将该蛋白转化为功能性 mRNA 输出因子，可在病毒感染期间替代 pUL69。
Transfer of the UAP56 interaction motif of human cytomegalovirus pUL69 to its murine cytomegalovirus homolog converts the protein into a functional mRNA export factor that can substitute for pUL69 during viral infection.
机构信息
Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Erlangen, Germany.
出版信息
J Virol. 2012 Jul;86(13):7448-53. doi: 10.1128/JVI.00730-12. Epub 2012 May 2.
Abstract
Nucleocytoplasmic shuttling and interaction with the cellular mRNA export factor UAP56 are prerequisites for the mRNA export activity of human cytomegalovirus (HCMV) pUL69. Although the murine cytomegalovirus homolog pM69 shuttles, it fails to export mRNAs due to its inability to recruit UAP56. However, chimeric proteins comprising pM69 fused to N-terminal pUL69 fragments, including its UAP56 interaction motif, acquire mRNA export activity. Importantly, growth curves of recombinant HCMVs illustrate that such a chimeric protein, but not pM69, substitutes for pUL69 during HCMV infection.
摘要
核质穿梭和与细胞 mRNA 输出因子 UAP56 的相互作用是人类巨细胞病毒 (HCMV) pUL69 的 mRNA 输出活性的前提条件。尽管鼠巨细胞病毒同源物 pM69 穿梭，但由于无法招募 UAP56，它无法输出 mRNAs。然而，包含 pM69 与 N 端 pUL69 片段融合的嵌合蛋白，包括其 UAP56 相互作用基序，获得了 mRNA 输出活性。重要的是，重组 HCMV 的生长曲线表明，在 HCMV 感染期间，这种嵌合蛋白而不是 pM69 替代 pUL69。
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