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Vol. 13, Issue 3, 915-929, March 2002

FBI-1 Can Stimulate HIV-1 Tat Activity and Is Targeted to a Novel Subnuclear Domain that Includes the Tat-P-TEFbcontaining Nuclear Speckles

P. Shannon Pendergrast,^* Chen Wang, Nouria Hernandez,^§ and Sui Huang

 ^*Cold Spring Harbor Laboratory and  ^§Howard Hughes Medical Institute, Cold Spring Harbor, New York 11724; and  Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611

FBI-1 is a cellular POZ-domain-containing protein that binds to the HIV-1 LTR and associates with the HIV-1 transactivator protein Tat. Here we show that elevated levels of FBI-1 specifically stimulate Tat activity and that this effect is dependent on the same domain of FBI-1 that mediates Tat-FBI-1 association in vivo. FBI-1 also partially colocalizes with Tat and Tat's cellular cofactor, P-TEFb (Cdk9 and cyclin T1), at the splicing-factor-rich nuclear speckle domain. Further, a less-soluble population of FBI-1 distributes in a novel peripheral-speckle pattern of localization as well as in other nuclear regions. This distribution pattern is dependent on the FBI-1 DNA binding domain, on the presence of cellular DNA, and on active transcription. Taken together, these results suggest that FBI-1 is a cellular factor that preferentially associates with active chromatin and that can specifically stimulate Tat-activated HIV-1 transcription.

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Corresponding author. Present address: Archemix Corp., 1 Hampshire St., Cambridge, MA 02139; e-mail address: pendergrast{at}archemix.com.

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Molecular Biology of the Cell
Vol. 13, 915-929, March 2002
Copyright © 2002 by The American Society for Cell Biology

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