TAR-RNA binding by HIV-1 Tat protein is selectively inhibited by its L-enantiomer.
AUTOR(ES)
Garbesi, A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=147661Documentos Relacionados
- Rotational symmetry in ribonucleotide strand requirements for binding of HIV-1 Tat protein to TAR RNA.
- HIV-1 tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure.
- Identification of a novel HIV-1 TAR RNA bulge binding protein.
- Association of HIV-1 Tat with the cellular protein, Purα, is mediated by RNA
- A small circular TAR RNA decoy specifically inhibits Tat-activated HIV-1 transcription.