%0 Journal Article %T Subcellular localization of the interaction between the human immunodeficiency virus transactivator Tat and the nucleosome assembly protein 1. %+ Laboratory of Molecular Virology %+ Institut Pasteur de Montevideo %A de Marco, Alex %A Dans, Pablo D %A Knezevich, Anna %A Maiuri, Paolo %A Pantano, Sergio %A Marcello, Alessandro %Z This work (AM) was supported in part by a HFSP Young Investigators Grant, by the Italian FIRB program of the Ministero dell'Istruzione, Universita' e Ricerca of Italy, by the European Community FP6 STREP n. 012182 and by the AIDS Program of the Istituto Superiore di Sanita' of Italy. PD and SP were supported by ANII--Agencia Nacional de Investigacio ́n e Innovacio ́n, Programa de Apoyo Secto- rial a la Estrategia Nacional de Innovacio ́n--INNOVA URUGUAY (Agreement no. DCI--ALA/2007/19.040 between Uruguay and the European Commission and FCE_60/2007). %< avec comité de lecture %@ 0939-4451 %J Amino Acids %I Springer Verlag %V 38 %N 5 %P 1583-93 %8 2010-05 %D 2010 %R 10.1007/s00726-009-0378-9 %M 19888548 %Z Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] %Z Computer Science [cs]/Bioinformatics [q-bio.QM]Journal articles %X 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. %G English %L pasteur-00684217 %U https://riip.hal.science/pasteur-00684217 %~ RIIP %~ RIIP_MONTEVIDEO