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Journal of Virology, November 2001, p. 10359-10371, Vol. 75, No. 21
Paul-Ehrlich-Institut, D-63225 Langen,
Germany
Received 10 January 2001/Accepted 18 July 2001
It was recently reported that the human endogenous retrovirus
HTDV/HERV-K encodes the regulatory protein Rec (formerly designated Corf), which is functionally equivalent to the nuclear export adapter
proteins Rev of human immunodeficiency virus and Rex of human T-cell
leukemia virus. We have demonstrated that the Rec protein interacts
with a characteristic 429-nucleotide RNA element, the Rec-responsive
element (RcRE), present in the 3' long terminal repeat of HTDV/HERV-K
transcripts. In analogy to the Rev and Rex proteins, which have
distinct RNA binding sites in their responsive elements, we have
proposed that Rec may also have a defined binding site in the RcRE. In
this report, we demonstrate that not every HTDV/HERV-K copy present in
the human genome contains an active RcRE, and we characterize mutations
that abrogate Rec function. In addition, we demonstrate that Rec
function requires binding to a complex, folded RNA structure rather
than binding to a discrete specific binding site, in contrast to Rev
and Rex and their homologous responsive elements. We define four
stem-loop structures in the RcRE that are essential for Rec function.
Finally, we demonstrate that both Rev and Rex can mediate nuclear
export through the RcRE but that their binding sites are different from
each other and from that of Rec.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.21.10359-10371.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Rec (Formerly Corf) Function Requires Interaction
with a Complex, Folded RNA Structure within Its Responsive
Element rather than Binding to a Discrete Specific Binding
Site

*
Corresponding author. Mailing address:
Paul-Ehrlich-Institut, Paul-Ehrlich Str. 51-59, D-63225 Langen,
Germany. Phone: 49-6103-77340. Fax: 49-6103-771252. E-mail:
loero{at}pei.de.
Present address: Boehringer Ingelheim Austria, Vienna, Austria.
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