Equine infectious anemia virus transactivator is a homeodomain-type protein

被引:7
作者
Willbold, D
Metzger, AU
Sticht, H
Gallert, KC
Voit, R
Dank, N
Bayer, P
Krauss, G
Goody, RS
Rösch, P
机构
[1] Univ Bayreuth, Lehrstuhl Biopolymere, D-95440 Bayreuth, Germany
[2] Univ Bayreuth, Lehrstuhl Biochem, D-95440 Bayreuth, Germany
[3] Deutsch Krebsforschungszentrum Mol Biol Zelle, D-69120 Heidelberg, Germany
[4] Max Planck Inst Mol Physiol, D-44139 Dortmund, Germany
关键词
EIAV; Tat; protein-DNA-complex; NMR; homeodomain;
D O I
10.1006/jmbi.1998.1636
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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), and specific binding of the equine anemia virus (EIAV) Tat Protein to a target TAR RNA is suggested by mutational analysis of the TAR RNA. Structural data on equine infectious anemia virus Tat protein reveal a helix-loop-helix-turn-helix limit structure very similar to homeobox domains that are known to bind specifically to DNA. Here we report results of gel-shift and foot printing analysis as well as fluorescence and nuclear magnetic resonance spectroscopy experiments that clearly show that EIAV Tar protein binds to DNA specifically at the long terminal repeat Pu.1 (GTTCCTGTTTT) and AP-1 (TGACGCG) sites, and thus suggest a common mechanism for the action of some of the known lentiviral Tat Proteins via the AP-1 initiator site. Complex formation with DNA induces specific shifts of the proton NMR resonances originating from amino acids in the core and basic domains of the protein. (C) 1998 Academic Press Limited.
引用
收藏
页码:749 / 755
页数:7
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