Key result
The affinity of HIV-1 Tat protein for the L-enantiomer of TAR RNA was identical to its affinity for the natural D-enantiomer, suggesting a binding model independent of RNA handedness.
The interaction of the flexible Tat protein with TAR RNA depends strongly on the tertiary structure of a binding pocket but not on its handedness.
An oligoribonucleotide, corresponding to the Tat-interactive top half of the HIV-1 TAR RNA stem-loop, was synthesized in both the natural D- and the enantiomeric L-configurations. The affinity of Tat for the two RNAs, assessed by competition binding experiments, was found to be identical and is reduced 10-fold for both, upon replacement of the critical bulge residue U23 with cytidine. It is suggested that this interaction of the flexible Tat protein depends strongly upon the tertiary structure of a binding pocket within TAR, but not upon its handedness, and may be described by a 'hand-in-mitten' model.
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Garbesi et al. (1998) studied HIV-1. L-enantiomer of TAR RNA vs. D-enantiomer of TAR RNA was evaluated on Binding affinity of Tat for TAR RNA. The affinity of HIV-1 Tat protein for the L-enantiomer of TAR RNA was identical to its affinity for the natural D-enantiomer, suggesting a binding model independent of RNA handedness.
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