A C-terminal domain in the avian sarcoma-leukosis virus pol gene product is not essential for viral replication.

The virion proteins encoded by the avian retroviral pol gene (reverse transcriptase and endonuclease) are formed by the proteolytic processing of a gag-pol fusion protein precursor. Recent studies have predicted that the avian sarcoma-leukosis virus pol precursor protein undergoes a previously undetected processing event resulting in the formation of common C termini for the endonuclease (pp32) and the beta subunit of reverse transcriptase (F. Alexander, J. Leis, D. A. Soltis, R. M. Crowl, W. Danho, M. S. Poonian, Y.-C. E. Pan, and A. M. Skalka, J. Virol. 61:534-542, 1987; D. Grandgenett, T. Quinn, P. J. Hippenmeyer, and S. Oroszlan, J. Biol. Chem. 260:8243-8249, 1985). This processing event removes 37 amino acids, thus defining a new pol domain. In this report, we present evidence that this C-terminal domain is translated as part of the gag-pol precursor but is not required for replication of the virus in tissue culture cells.