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.
Complete list of metadatas

https://hal-riip.archives-ouvertes.fr/pasteur-00684217
Contributor : Mariella Botta <>
Submitted on : Friday, March 30, 2012 - 9:52:08 PM
Last modification on : Friday, July 5, 2019 - 3:22:01 PM

Links full text

Identifiers

Collections

Citation

Alex de Marco, Pablo D Dans, Anna Knezevich, Paolo Maiuri, Sergio Pantano, et al.. Subcellular localization of the interaction between the human immunodeficiency virus transactivator Tat and the nucleosome assembly protein 1.. Amino Acids, Springer Verlag, 2010, 38 (5), pp.1583-93. ⟨10.1007/s00726-009-0378-9⟩. ⟨pasteur-00684217⟩

Share

Metrics

Record views

132