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Nucleic Acids Research, 1993, Vol. 21, No. 1 151-154
© 1993

MOLECULAR BIOLOGY

Rotational symmetry in ribonucleotide strand requirements for binding of HIV-1 Tat protein to TAR RNA

Richard W. Barnett, Ulrike Delling, Raya Kuperman, Nahum Sonenberg1,2 and Martin Sumner-Smith*

Allelix Biopharmaceuticals Inc., 6850 Goreway Drive, Mississauga, Ontario L4V 1P1, Canada 1Department of Biochemistry, McGill University Montreal, Quebec H3G 1Y6, Canada 2McGill Cancer Centre, McGill University Montreal, Quebec H3G 1Y6, Canada

* To whom correspondence should be addressed

Received July 27, 1992. Accepted November 24, 1992.

Transactivation of human immunodeficiency vims (HIV) gene expression requires binding of the viral Tat protein to a RNA hairpin-loop structure (TAR) which contains a two or three-nucleotide bulge. Tat binds in the vicinity of the bulge and the two adjacent duplex stems, recognising both specific sequence and structural features of TAR. Binding is mediated by an arginine-rlch domain, placing Tat in the family of arginine-rich RNA binding proteins that includes other transactivators, virus capsid proteins and ribosome binding proteins. In order to determine what features of TAR allow Tat to bind efficiently to RNA but not DNA forms, we examined Tat binding to a series of RNA-DNA hybrids. We found that only one specific strand in each duplex stem region needs to be RNA, implying that interaction between Tat and a given stem may be solely or predominantly with one of the two strands. However, the essential strand is not the same one for each stem, suggesting a switch in the bound strand on opposing sides of the bulge.


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