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首页> 外文期刊>Molecular and Cellular Biology >Characterization of the nuclear export signal of human T-cell lymphotropic virus type 1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions.
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Characterization of the nuclear export signal of human T-cell lymphotropic virus type 1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions.

机译：1型人类T细胞淋巴病毒Rex的核输出信号的特征表明，核输出是由位置可变的疏水相互作用介导的。

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We previously determined that amino acids 64 to 120 of human T-cell lymphotropic virus type 1 (HTLV-1) Rex can restore the function of an effector domain mutant of human immunodeficiency virus type 1 (HIV-1) Rev (T. J. Hope, B. L. Bond, D. McDonald, N. P. Klein, and T. G. Parslow, J. Virol. 65:6001-6007, 1991). In this report, we (i) identify and characterize a position-independent 17-amino-acid region of HTLV-1 Rex that fully complements HIV-1 Rev effector domain mutants and (ii) show that this 17-amino-acid region and specific hydrophobic substitutions can serve as nuclear export signals. Mutagenesis studies revealed that four leucines within the minimal region were essential for function. Alignment of the minimal Rex region with the HIV-1 Rev effector domain suggested that the position of some of the conserved leucines is flexible. We found two of the leucines could each occupy one of two positions within the context of the full-length HTLV-1 Rex protein and maintain function. The idea of flexibility within the Rex effector domain was confirmed and extended by identifying functional substitutions by screening a library of effector domain mutants in which the two regions of flexibility were randomized. Secondly, the functional roles of the minimal Rex effector domain and hydrophobic substitutions were independently confirmed by demonstrating that these effector domains could serve as nuclear export signals when conjugated with bovine serum albumin. Nuclear export of the wild-type Rex conjugates was temperature dependent and sensitive to wheat germ agglutinin and was blocked by a 20-fold excess of unlabeled conjugates. Together, these studies reveal that position-variable hydrophobic interactions within the HTLV-1 Rex effector domain mediate nuclear export function.
机译：我们先前确定，人类T细胞1型淋巴病毒（HTLV-1）Rex的64至120位氨基酸可以恢复人类免疫缺陷病毒1型（HIV-1）Rev（TJ Hope，BL）的效应子域突变体的功能。 Bond，D.McDonald，NP Klein和TG Parslow，J.Virol.65：6001-6007，1991）。在本报告中，我们（i）鉴定和表征与LV-1 Rev效应子域突变体完全互补的HTLV-1 Rex的位置无关的17个氨基酸区域，并且（ii）显示该17个氨基酸区域和特定的疏水取代可以充当核输出信号。诱变研究表明，最小区域内的四个亮氨酸对于功能至关重要。最小Rex区域与HIV-1 Rev效应子域的比对表明，某些保守的亮氨酸的位置是灵活的。我们发现，两个亮氨酸可能各自在全长HTLV-1 Rex蛋白的背景下占据两个位置之一，并保持功能。通过筛选效应子结构域突变体的文库来鉴定功能取代，从而确认并扩展了Rex效应子域内的柔性构想，在该库中，两个柔性域是随机的。其次，通过证明当与牛血清白蛋白结合时，这些效应子结构域可以充当核输出信号，独立地证实了最小的Rex效应子结构域和疏水取代的功能性作用。野生型雷克斯结合物的核输出是温度依赖性的并且对小麦胚芽凝集素敏感，并且被20倍过量的未标记结合物阻断。总之，这些研究表明HTLV-1 Rex效应子域内位置可变的疏水相互作用介导了核输出功能。

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