ArticlePloS one2014
Conserved arginines of bovine adenovirus-3 33K protein are important for transportin-3 mediated transport and virus replication.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- RETRACTED: Regions of Bovine Adenovirus-3 Protein VII Involved in Interactions with Viral and Cellular Proteins.Viruses · 2024Article
- Article
- Nuclear and Nucleolar Localization of Bovine Adenovirus-3 Protein V.Frontiers in microbiology · 2020Article
- Splicing-Dependent Subcellular Targeting of Borna Disease Virus Nucleoprotein Isoforms.Journal of virology · 2019Article
- Identification and characterization of nuclear and nucleolar localization signals in the adeno-associated virus serotype 2 assembly-activating protein.Journal of virology · 2015Article
- Regulation of human adenovirus alternative RNA splicing by the adenoviral L4-33K and L4-22K proteins.International journal of molecular sciences · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The L6 region of bovine adenovirus (BAdV)-3 encodes a spliced protein designated 33K. The 33K specific sera detected five major proteins and three minor proteins in transfected or virus infected cells, which could arise by internal initiation of translation and alternative splicing. The 33K protein is predominantly localized to the nucleus of BAdV-3 infected cells. The 33K nuclear transport utilizes both classical importin-α/-β and importin-β dependent nuclear import pathways and preferentially binds to importin-α5 and transportin-3 receptors, respectively. Analysis of mutant 33K proteins demonstrated that amino acids 201-240 of the conserved C-terminus of 33K containing RS repeat are required for nuclear localization and, binding to both importin-α5 and transportin-3 receptors. Interestingly, the arginine residues of conserved RS repeat are required for binding to transportin-3 receptor but not to importin-α5 receptor. Moreover, mutation of arginines residues of RS repeat proved lethal for production of progeny virus. Our results suggest that arginines of RS repeat are required for efficient nuclear transport of 33K mediated by transportin-3, which appears to be essential for replication and production of infectious virion.
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