TOLERANCE OF DIVERSE AMINO-ACID SUBSTITUTIONS AT CONSERVED POSITIONS IN THE NUCLEAR EXPORT SIGNAL (NES) OF HIV-1 REV

The effector domain of the Rev protein is a nuclear export signal (NES ) that is responsible for transporting Rev and its bound congeners out of the nucleus and into the cytoplasm. Previous work has identified s everal critical residues in the NES and has led to the belief that NES s of the Rev type are necessarily leucine rich. Here we present the se quences of a large number of functional Rev molecules with NES mutatio ns. The data indicate a previously unreported diversity in allowable r esidues at a number of positions, including each of the leucine residu es previously considered essential. (C) 1998 Academic Press.