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Subcellular Localization of Novel Stress Protein VISP  

Moon, Chang-Hoon (Department of Biological Sciences, University of Ulsan)
Yoon, Won-Joon (Department of Biological Sciences, University of Ulsan)
Ko, Myoung-Seok (Department of Biological Sciences, University of Ulsan)
Kim, Hyun-Ju (Division of Molecular and Life Sciences, Pohang University of Science and Technology (POSTECH))
Park, Jeong-Woo (Department of Biological Sciences, University of Ulsan)
Publication Information
Korean Journal of Microbiology / v.42, no.4, 2006 , pp. 271-276 More about this Journal
Abstract
Previously we demonstrated that virus-inducible stress protein (VISP) is induced in fish cells by the infection of a fish rhabdovirus. In this paper, we investigated the subcellular localization of the VISP and determined the region of VISP responsible for the subcellular localization. The CHSE-214 cells were stained with monoclonal antibody raised against VISP and observed with confocal microscope to detect the endogenous VISP. The results showed that the VISP localizes to the perinuclear region as spots. A plasmid expressing VISP fused to enhanced green fluorescent protein (EGFP) was constructed. The transient expression of full-length VISP fused to EGFP in CHSE-214 cells confirmed the spot formation of the VISP at perinuclear region. To determine the region responsible for the perinuclear localization of the VISP, we constructed a series of deletion mutants and, by using these deletion mutants, we found that C-terminal region of the VISP (aa 612-710) is essential for the perinuclear distribution of VISP and that this region contained nuclear receptor binding motif (691-TLTSLLL-697). Our results suggest that VISP localizes to the perinuclear region and C-terminal regions are important for this localization. Further studies on the role of the perinuclear localization of VISP in IHNV growth mali reveal the novel mechanism of IHNV pathogenecity.
Keywords
EGFP fusion protein; subcellular localization; VISP;
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