Expression of human endogenous retrovirus K (HERV-K) is associated with germ-cell neoplasia. HERV-K encodes a protein of the Rev/Rex family, cORF, that supports cellular transformation and binds the promyelocytic leukemia zinc finger (PLZF) protein implicated in spermatogenesis. Rev/Rex function invariably depends on multimerization. Here we show that cORF likewise self-associates to form higher-order oligomers. Amino acids (aa) 47-87 in cORF are sufficient, aa 75-87 essential for self-association. Consistently, this domain is predicted to form a hydrophobic α-helix that may represent an oligomerization interface. The existence of a dimerization-competent cORF mutant lacking PLZF-binding activity (cORF47-87) suggests a way of dominant negative inhibition of the proposed tumor susceptibility factor cORF. © 2001 Federation of European Biochemical Societies.
Boese, A., Galli, U., Geyer, M., Sauter, M., & Mueller-Lantzsch, N. (2001). The Rev/Rex homolog HERV-K cORF multimerizes via a C-terminal domain. FEBS Letters, 493(2–3), 117–121. https://doi.org/10.1016/S0014-5793(01)02280-3