Premium
The Rev/Rex homolog HERV‐K cORF multimerizes via a C‐terminal domain
Author(s) -
Boese Annette,
Galli Uwe,
Geyer Matthias,
Sauter Marlies,
Mueller-Lantzsch Nikolaus
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02280-3
Subject(s) - zinc finger , mutant , biology , amino acid , chemistry , microbiology and biotechnology , function (biology) , transcription factor , genetics , gene
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.