Abstract
The HIV-1 Rev protein increases the cytoplasmic levels of unspliced and singly spliced target transcripts in metazoan systems. Based on experiments that indicate a similar function of Rev in the yeast S. cerevisiae, we have identified a yeast protein that interacts with the effector domain of Rev. The protein, Rip1p, is a novel small nucleoporin-like protein, some of which is associated with nuclear pores. Its closest known yeast relative is a nuclear pore component also implicated in mRNA transport from nucleus to cytoplasm. Analysis of strains that overexpress Riplp or that are deleted for the
RIP1 gene show that Rip1p is important for the effect of Rev on gene expression, indicating that the physical interaction is of functional significance in vivo. The results suggest that Rev directly promotes the cytoplasmic transport of suitable transcripts by targeting them to the nuclear pore.