The Rev protein of HIV-1 is essential for HIV-1 proliferation due to its role in exporting viral RNA from the nucleus. We used a modified version of tandem affinity purification (TAP) tagging to identify proteins interacting with HIV-1 Rev in human cells and discovered a prominent interaction between Rev and nucleosome assembly protein 1 (Nap1). This interaction was also observed by specific retention of Nap1 from human cell lysates on a Rev affinity column. Nap1 was found to bind Rev through the Rev arginine-rich domain and altered the oligomerization state of Rev in vitro. Overexpression of Nap1 stimulated the ability of Rev to export RNA, reduced the nucleolar localization of Rev, and affected Rev nuclear import rates. The results suggest that Nap-1 may influence Rev function by increasing the availability of Rev.

中文翻译：

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HIV Rev和核小体组装蛋白NAP1之间稳定的复合物形成会影响Rev功能。

HIV-1的Rev蛋白对于HIV-1的增殖至关重要，因为它在从细胞核输出病毒RNA中起着重要的作用。我们使用串联亲和纯化（TAP）标签的修改后的版本来识别与人类细胞中HIV-1 Rev相互作用的蛋白质，并发现Rev与核小体组装蛋白1（Nap1）之间存在显着相互作用。还通过在Rev亲和力柱上将Nap1从人细胞裂解物中特异性保留来观察到这种相互作用。Nap1被发现通过Rev精氨酸丰富域绑定Rev，并在体外改变Rev的低聚状态。Nap1的过表达刺激Rev出口RNA的能力，减少Rev的核仁定位，并影响Rev的核导入率。结果表明，Nap-1可能通过提高Rev的可用性来影响Rev功能。