Open AccessEquine infectious anemia virus Tat is a predominantly helical protein
Author(s) -
STICHT Heinrich,
WILLBOLD Dieter,
BAYER Peter,
EJCHART Andrzej,
HERRMANN Franz,
ROSINARBESFELD Rina,
GAZIT Ara,
YANIV Abraham,
FRANK Rainer,
RÖSCH Paul
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb18455.x
Subject(s) - equine infectious anemia , protein secondary structure , virology , rna , protein structure , biology , virus , chemistry , genetics , gene , biochemistry
Nuclear magnetic resonance (NMR) spectroscopy revealed features of the secondary structure of the equine infectious anemia virus (EIAV) Tat protein in solution. We could show that this protein, which is required in the replication cycle of lentiviruses, forms a predominantly helical structure in trifluoroethanol/water (40% by vol.) solution. In particular, the basic RNA‐binding region and the adjacent core domain, which are highly conserved among lentiviral Tat proteins, show helix‐type secondary structure under these conditions. Our observations, in concert with recent biochemical data from other laboratories, suggest that the core sequence region and the basic sequence region form interdependent structural domains, both possibly necessary for correct RNA binding.