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Molecular and Cellular Biology, February 1999, p. 1210-1217, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Arginine-Rich Domains Present in Human Immunodeficiency Virus Type 1 Tat and Rev Function as Direct Importin beta -Dependent Nuclear Localization Signals

Ray Truant and Bryan R. Cullen*

Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710

Received 17 August 1998/Returned for modification 14 October 1998/Accepted 27 October 1998

Protein nuclear import is generally mediated by basic nuclear localization signals (NLSs) that serve as targets for the importin alpha  (Imp alpha ) NLS receptor. Imp alpha  is in turn bound by importin beta  (Imp beta ), which targets the resultant protein complex to the nucleus. Here, we report that the arginine-rich NLS sequences present in the human immunodeficiency virus type 1 regulatory proteins Tat and Rev fail to interact with Imp alpha  and instead bind directly to Imp beta . Using in vitro nuclear import assays, we demonstrate that Imp alpha  is entirely dispensable for Tat and Rev nuclear import. In contrast, Imp beta  proved both sufficient and necessary, in that other beta -like import factors, such as transportin, were unable to support Tat or Rev nuclear import. Using in vitro competition assays, it was demonstrated that the target sites on Imp beta  for Imp alpha , Tat, and Rev binding either are identical or at least overlap. The interaction of Tat and Rev with Imp beta  is also similar to Imp alpha  binding in that it is inhibited by RanGTP but not RanGDP, a finding that may in part explain why the interaction of the Rev nuclear RNA export factor with target RNA species is efficient in the cell nucleus yet is released in the cytoplasm. Together, these studies define a novel class of arginine-rich NLS sequences that are direct targets for Imp beta  and that therefore function independently of Imp alpha .

* Corresponding author. Mailing address: Box 3025, Room 426, CARL Building, Research Drive, Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-3369. Fax: (919) 681-8979. E-mail: Culle002{at}mc.duke.edu.

Molecular and Cellular Biology, February 1999, p. 1210-1217, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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