Dissection of the proposed base triple in human immunodeficiency virus TAR RNA indicates the importance of the Hoogsteen interaction. NLM AIDSLINE Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

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Dissection of the proposed base triple in human immunodeficiency virus TAR RNA indicates the importance of the Hoogsteen interaction.

Biochemistry. 1997 Mar 25;36(12):3491-5. Unique Identifier : AIDSLINE MED/97238548
Tao J; Chen L; Frankel AD; Department of Biochemistry and Biophysics, University of California,; San Francisco 94143-0448, USA.

Abstract: A single arginine residue within the RNA-binding domain of the human immunodeficiency virus Tat protein makes a critical sequence-specific contact to TAR RNA. Arginine as the free amino acid also binds specifically to TAR and induces a change in RNA conformation similar to that induced by Tat peptides. NMR and biochemical studies have suggested that the arginine-binding site is stabilized by a base triple interaction between a bulged U and an A x U base pair in the adjacent stem. In this study, we have used chemical modification and mutagenesis experiments to examine the relative contributions of the Watson-Crick and Hoogsteen base-pairing partners of the proposed U-A x U base triple. We show that the Hoogsteen interaction is critical for arginine binding whereas the Watson-Crick interaction can be eliminated or replaced by other base-base interactions. The results are consistent with biochemical studies of the Tat-TAR interaction and support the base triple model for the structure of TAR.
Keywords: *Gene Products, tat/METABOLISM *HIV Long Terminal Repeat *HIV-1 *Models, Chemical *RNA, Viral/CHEMISTRYKWDgeneproducts,tat/metabolismKWDhivlongterminalrepeatKWDhiv-1KWDmodels,chemicalKWDrna,viral/chemistry
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Copyright © 1997 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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