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Journal of Virology, March 1999, p. 2193-2200, Vol. 73, No. 3
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Intracellular Redistribution of Truncated La
Protein Produced by Poliovirus 3Cpro-Mediated
Cleavage
Kazuko
Shiroki,1,*
Takeshi
Isoyama,1
Shusuke
Kuge,1
Toshihiko
Ishii,1
Shinobu
Ohmi,2
Syoji
Hata,3
Koichi
Suzuki,3
Yoshinari
Takasaki,4 and
Akio
Nomoto1
Department of
Microbiology1 and
Department of
Bacterial Infection,2 Institute of Medical
Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo
108-8639, Institute of Molecular and Cellular Biosciences,
University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo
113-0032,3 and
Division of Rheumatology,
Department of Medicine, Juntendo University School of Medicine,
3-1-3 Hongo, Bunkyo-ku, Tokyo 113-8421,4 Japan
Received 29 June 1998/Accepted 16 November 1998
The La autoantigen (also known as SS-B), a cellular RNA binding
protein, may shuttle between the nucleus and cytoplasm, but it is
mainly located in the nucleus. La protein is redistributed to the
cytoplasm after poliovirus infection. An in vitro translation study
demonstrated that La protein stimulated the internal initiation of
poliovirus translation. In the present study, a part of the La protein
was shown to be cleaved in poliovirus-infected HeLa cells, and this
cleavage appeared to be mediated by poliovirus-specific protease 3C
(3Cpro). Truncated La protein (dl-La) was produced in vitro
from recombinant La protein by cleavage with purified 3Cpro
at only one Gln358-Gly359 peptide bond in the
408-amino-acid (aa) sequence of La protein. The dl-La expressed in L
cells was detected in the cytoplasm. However, green fluorescence
protein linked to the C-terminal 50-aa sequence of La protein was
localized in the nucleus, suggesting that this C-terminal region
contributes to the steady-state nuclear localization of the intact La
protein in uninfected cells. The dl-La retained the enhancing activity of translation initiation driven by poliovirus RNA in rabbit
reticulocyte lysates. These results suggest that La protein is cleaved
by 3Cpro in the course of poliovirus infection and that the
dl-La is redistributed to the cytoplasm. dl-La, as well as La protein,
may play a role in stimulating the internal initiation of poliovirus
translation in the cytoplasm.
*
Corresponding author. Mailing address: Department of
Microbiology, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. Phone:
81-3-5449-5503. Fax: 81-3-5449-5408. E-mail:
kshiroki{at}ims.u-tokyo.ac.jp.
Journal of Virology, March 1999, p. 2193-2200, Vol. 73, No. 3
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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