Formation of trans-activation competent HIV-1 Rev:RRE complexes requires the recruitment of multiple protein activation domains.

摘要: The HIV-1 Rev trans-activator is a nucleocytoplasmic shuttle protein that essential for virus replication. directly binds to unspliced and incompletely spliced viral RNA via the cis-acting Response Element (RRE) sequence. Subsequently, oligomerizes cooperatively interacts with cellular nuclear export receptor CRM1. In addition mediating export, also affects stability, translation packaging of Rev-bound transcripts. Although it established function requires multimeric assembly molecules on RRE, relatively little known about how many monomers are sufficient form trans-activation competent Rev:RRE complex, or which specific activity affected by its oligomerization. We here analyzed functional studies homooligomer formation capacity this regulatory protein. gain-of-function approach, we fused various heterologous dimerization domains an otherwise oligomerization-defective mutant were able demonstrate oligomerization not required per se trans-activator. contrast, however, oligomers RRE precondition affecting Rev-regulated mRNA. Moreover, experimental evidence provided showing at least two activation complexes. presented data further refine model demonstrating thereby recruiting domains, RNA.