BIOINFORMATICS<-->STRUCTURE
Jerusalem, Israel, November 17-21, 1996

Abstract

The equine infectious anemia virus transactivator protein is a DNA binding protein

Dieter Willbold (1), Armin U. Metzger (1), Karl Christian Gallert (2), Norbert Dank (2), Peter Bayer (3), Rina Rosin-Arbesfeld (4), Abraham Yaniv (4), Arnona Gazit (4), Roger Goody (3), Gerhard Krauss (2) and Paul Roesch (1)

(1) Lehrstuhl fuer Struktur und Chemie der Biopolymere und
(2) Lehrstuhl fuer Biochemie, Universitaet Bayreuth, D-95440 Bayreuth, Germany;
(3) Max-Planck-Institut fuer molekulare Physiologie, D-44026 Dortmund, Germany;
(4) Tel-Aviv University, Sackler School of Medicine, Department of Human Microbiology, Ramat-Aviv, 69978 Tel-Aviv, Israel

Dieter.Willbold@uni-bayreuth.de

Lentiviral transactivator (tat) proteins are essential for viral replication. Tat proteins of human immunodeficiency virus type 1 and bovine immunodeficiency virus form complexes with their respective RNA targets (tat responsive element, TAR). By analogy, RNA-binding capability was inferred for the equine infectious anemia virus (EIAV) tat protein (e-tat). However, specific binding of e-tat and the respective TAR RNA was never shown conclusively. In addition, structural data lead to the suggestion of e-tat showing a helix-turn-helix limit structure analogous to homeobox domain proteins, that are known to bind DNA. In the present work, using fluorescence titration, gel retardation assays and nuclease protection analysis, we show that e-tat indeed binds to an upstream DNA sequence element within the EIAV long terminal repeat.

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