 |
Journal articles
Subcellular localization of the interaction between the human immunodeficiency virus transactivator Tat and the nucleosome assembly protein 1.
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 requires hNAP-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.
https://hal-riip.archives-ouvertes.fr/pasteur-00684217
Contributor : Mariella Botta Connect in order to contact the contributor
Submitted on : Friday, March 30, 2012 - 9:52:08 PM
Last modification on : Friday, July 5, 2019 - 3:22:01 PM
Contributor : Mariella Botta Connect in order to contact the contributor
Submitted on : Friday, March 30, 2012 - 9:52:08 PM
Last modification on : Friday, July 5, 2019 - 3:22:01 PM
Links full text
