Stable complex formation between HIV Rev and the nucleosome assembly protein, NAP1, affects Rev function

作者：Cochrane Alan; Murley Laura Lea; Gao Mian; Wong Raymond; Clayton Kiera; Brufatto Nicole; Canadien Veronica; Mamelak Daniel; Chen Tricia; Richards Dawn; Zeghouf Mahel; Greenblatt Jack; Burks Christian; Frappier Lori^*

来源：Virology, 2009, 388(1): 103-111.

DOI：10.1016/j.virol.2009.03.005

• Rev
• HIV
• Nucleosome assembly protein
• Nucleolar localization
• TAP-tagging

The Rev protein of HIV-1 is essential for HIV-1 proliferation due to its role in exporting viral RNA front 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.

• 出版日期2009-5-25