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Originally published In Press as doi:10.1074/jbc.M104830200 on August 14, 2001

J. Biol. Chem., Vol. 276, Issue 42, 39220-39225, October 19, 2001
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Visualization of in Vivo Direct Interaction between HIV-1 TAT and Human Cyclin T1 in Specific Subcellular Compartments by Fluorescence Resonance Energy Transfer*

Alessandro MarcelloDagger §, Riccardo A. G. Cinelli§, Aldo Ferrari§, Anna SignorelliDagger §||, Mudit TyagiDagger §, Vittorio Pellegrini§, Fabio Beltram§, and Mauro GiaccaDagger §**

From the Dagger  Molecular Medicine Laboratory, International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34012 Trieste, Italy and § NEST-INFM and Scuola Normale Superiore, Piazza dei Cavalieri 7, 56126 Pisa, Italy

Human cyclin T1, a component of the P-TEFb kinase complex, was originally identified through its biochemical interaction with the Tat transactivator protein of human immunodeficiency virus type 1 (HIV-1). Current understanding suggests that binding of Tat to P-TEFb is required to promote efficient transcriptional elongation of viral RNAs. However, the dynamics and the subnuclear localization of this process are still largely unexplored in vivo. Here we exploit high resolution fluorescence resonance energy transfer (FRET) to visualize and quantitatively analyze the direct interaction between Tat and cyclin T1 inside the cells. We observed that cyclin T1 resides in specific subnuclear foci which are in close contact with nuclear speckles and that Tat determines its redistribution outside of these compartments. Consistent with this observation, strong FRET was observed between the two proteins both in the cytoplasm and in regions of the nucleus outside of cyclin T1 foci and overlapping with Tat localization. These results are consistent with a model by which Tat recruits cyclin T1 outside of the nuclear compartments where the protein resides to promote transcriptional activation.

* This work was supported by grants from the National Research Program on AIDS of the Istituto Superiore di Sanità (to M. G. and A. M.) and from Ministero dell'Istruzione, Universita' e Ricerca (to M. G. and F. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Contributed equally to the results of this work.

|| Supported by INFM within the framework of a training grant of the European Social Fund and the Italian Ministero del Lavoro. Present address: Data Medica SpA, Padova, Italy.

** To whom correspondence should be addressed: Molecular Medicine Laboratory, ICGEB, Padriciano 99, 34012 Trieste, Italy. Tel.: 39-040-3757-324; Fax: 39-040-226555; E-mail: giacca@icgeb.trieste.it.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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