Abstract
The yeast two-hybrid system was used to characterize homomeric interactions between the Gag proteins of Rous sarcoma virus (RSV). The RSV Gag precursor was found to interact strongly with itself and not with various control proteins. The RSV Gag did not interact significantly with Gag proteins of a variety of other retroviruses, including murine leukemia viruses and primate lentiviruses. Deletion analysis suggested that two nonoverlapping regions are independently sufficient to mediate RSV Gag-Gag dimerization. One such region lies near the N terminus and contains p2, p10, and a large N-terminal part of the capsid (CA) domain; the other is localized in the C terminus and includes a small C-terminal portion of CA and the nucleocapsid protein. These interaction domains may play roles in viral assembly.