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J. Biol. Chem., Vol. 277, Issue 7, 5308-5314, February 15, 2002
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From the Department of Mammalian Virology, Institute for Animal
Science and Health (ID-Lelystad), P.O. Box 65, 8200 AB, Lelystad,
The Netherlands and Pepscan Systems, Inc., P.O. Box 2098, 8203 AB Lelystad, The Netherlands
The pestivirus envelope glycoprotein
Erns has RNase activity and therefore was suspected
to enter cells to cleave RNA. The protein contains an RNase domain with
a C-terminal extension, which shows homology with a membrane-active
peptide. The modular architecture and the C-terminal homology suggested
that the C terminus could be responsible for the presumed
translocation. Peptides corresponding to the C-terminal domain of
Erns and also the homologous L3 loop of ribotoxin II were
indeed able to translocate across the eukaryotic cell membrane and were
targeted to the nucleoli. The entire Erns protein was also
able to translocate into the cell. Furthermore, other labeled proteins
and even active enzymes could be transported inside the cell when they
were attached to the C-terminal Erns peptide. Translocation
was energy-independent and not mediated by a protein receptor. The
peptides showed no specificity for cell type or species.
Translocation Activity of C-terminal Domain of Pestivirus
Erns and Ribotoxin L3 Loop*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Mammalian
Virology, Inst. for Animal Science and Health (ID-Lelystad), Edelhertweg 15, P.O. Box 65, 8200 AB, Lelystad, The Netherlands. Tel.:
31-320-238271; Fax: 31-320-238120; Email:
j.p.m.langedijk@id.wag-ur.nl.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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