Nucleic Acids Research, 1990, Vol. 18, No. 7 1839-1846
© 1990
MOLECULAR BIOLOGY |
Efficient trans-activation by the HIV-2 Tat protein requires a duplicated TAR RNA structure
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases Bethesda, MD 20892, USA
* To whom correspondence should be addressed a NIAID-NIH, Building 4, Room 307, Bethesda, MD 20892, USA
Received October 23, 1989. Revised February 28, 1990. Accepted February 28, 1990.
Human immunodeficiency viruses HIV-1 and HIV-2 encode a Tat protein that activates transcription from the long terminal repeats. The target for trans-activation is termed the trans-acting responsive (TAR) element. TAR has an extensively folded RNA secondary structure and is present at the 5' end of all viral mRNAs. Considerable similarities exist between both Tat and TAR of the two viruses. The TAR element of HIV-2 (TAR-2) resembles a tandem duplication of the TAR-1 hairpin structure. Tat-2 conserves many of the protein domains in Tat-1, although it is slightly larger than its counterpart. Given the similarity between the two Tat proteins, it is somewhat unexpected that HIV-2 Tat (Tat-2) only poorly activates the heterologous TAR-1 element. Here, we tested whether the duplicated structure of TAR-2 is required for full Tat-2 activity. We show that the addition of a second TAR hairpin to TAR-1 increased its Tat-2 responsiveness by 3-fold.
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