Subcellular localization of the interaction between the human immunodeficiency virus transactivator Tat and the nucleosome assembly protein 1

Alex De Marco, Pablo D. Dans, Anna Knezevich, Paolo Maiuri, Sergio Pantano, Alessandro Marcello

Research output: Contribution to journalArticleResearchpeer-review

16 Citations (Scopus)

Abstract

The histone chaperone nucleosome assembly protein, hNAP-1, is a host cofactor for the activity of the human immunodeficiency virus type 1 (HIV-1) transactivator Tat. The interaction between these two proteins has been shown to be important for Tat-mediated transcriptional activation and for efficient viral infection. Visualization of HIV-1 transcription and fluorescence resonance energy transfer experiments performed in this work demonstrate that hNAP-1 is not recruited to the site of Tat activity but the two proteins interact at the nuclear rim. These data are consistent with a mechanism that requireshNAP-1 for the transport of Tat within the nucleus rather than for the remodeling of nucleosomes on the provirus. Protein-protein docking and molecular modeling of the complex suggest that this interaction occurs between the basic domain of Tat and the histone-binding domain. The combination of theoretical and whole cell studies provided new insights into the functional significance of the Tat:hNAP-1 recognition.

Original languageEnglish
Pages (from-to)1583-1593
Number of pages11
JournalAmino Acids
Volume38
Issue number5
DOIs
Publication statusPublished - 1 May 2010
Externally publishedYes

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