The Rev/Rex homolog HERV-K cORF multimerizes via a C-terminal domain.
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 alpha-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.
Boese
A
A
Institut für Medizinische Mikrobiologie und Hygiene, Abteilung, Virologie, Haus 47, 66421 Hamburg, Germany.
Galli
U
U
Geyer
M
M
Sauter
M
M
Mueller-Lantzsch
N
N
D019281:Dimerization; D020077:Endogenous Retroviruses / Q000737:chemistry / Q000235:genetics; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D009154:Mutation; D009373:Neoplasms, Germ Cell and Embryonal / Q000737:chemistry / Q000235:genetics; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020798:Two-Hybrid System Techniques; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
C406149:HERV-K cORF protein, Human endogenous retrovirus K; D014764:Viral Proteins