Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus.

Constitutive transport element (CTE) facilitates retroviral RNA export by interacting with the cellular RNA export machinery. Two cellular proteins, RNA helicase A (RHA) and Tip-associated protein (Tap) were identified as binding to CTE and were proposed to function as CTE co-factors (1,2). Here, we report that these two CTE-binding proteins interact with each other in vitro and in vivo. The in vitro binding of RHA to Tap is direct and independent of either CTE or the nuclear transport domain of RHA. The removal of the first 60 amino acids of Tap significantly diminishes the binding to RHA. The activity of this Tap mutant to enhance CTE-mediated gene expression is also markedly reduced. A transdominant mutant of Tap inhibited RHA-mediated up-regulation of CTE function in mammalian cells. The nuclear transport domain of RHA also interfered with Tap-mediated transactivation of the CTE function in quail cells, in which the function of CTE is dependent on the expression of a functional human Tap cDNA.