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Abstract
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Nuclear transport of plant potyviral proteins.

M A Restrepo, D D Freed, J C Carrington
M A Restrepo
Department of Biology, Texas A&M University, College Station 77843.
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D D Freed
Department of Biology, Texas A&M University, College Station 77843.
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J C Carrington
Department of Biology, Texas A&M University, College Station 77843.
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Published October 1990. DOI: https://doi.org/10.1105/tpc.2.10.987

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  • Copyright © 1990 by American Society of Plant Biologists

Abstract

We have used immunoblotting, immunocytochemical, and gene fusion methods to examine the differential subcellular partitioning of tobacco etch potyvirus proteins that are potentially associated with RNA replication. From the earliest timepoints at which viral proteins could be detected, proteins Nla (49-kilodalton proteinase) and Nlb (58-kilodalton polymerase) were localized primarily in the nucleus, whereas the 71-kilodalton cylindrical inclusion protein was identified in the cytoplasm. The Nla and Nlb coding regions were fused to the beta-glucuronidase (GUS) sequence in a plant expression vector, resulting in synthesis of chimeric proteins in transfected protoplasts and in transgenic plants. In situ localization of GUS activity revealed nuclear localization of the GUS-Nla and GUS-Nlb fusion proteins and cytoplasmic localization of nonfused GUS. These results indicate that both Nla and Nlb contain nuclear targeting signals, and that they may serve as useful models for studies of plant cell nuclear transport. A discussion of the general utility of the nuclear transport system described here, as well as the role of nuclear translocation of potyviral proteins, is presented.

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Nuclear transport of plant potyviral proteins.
M A Restrepo, D D Freed, J C Carrington
The Plant Cell Oct 1990, 2 (10) 987-998; DOI: 10.1105/tpc.2.10.987

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Nuclear transport of plant potyviral proteins.
M A Restrepo, D D Freed, J C Carrington
The Plant Cell Oct 1990, 2 (10) 987-998; DOI: 10.1105/tpc.2.10.987
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The Plant Cell
Vol. 2, Issue 10
Oct 1990
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