Abstract |
The dUTPase is a ubiquitous and crucial enzyme responsible for regulating cellular levels of dUTP. In the present study, the expression pattern and translocation of a dUTPase homolog encoded by Singapore grouper iridovirus (SGIV) were elucidated. The SGIV ORF049R encodes a dUTPase homolog, which is a peptide of 155 amino acids that contains five conserved motifs. The temporal expression pattern during infection in vitro revealed that the SGIV dUTPase was an early transcript. A leucine-rich nuclear export signal (NES) at the C-terminus was predicted using CBS Online Servers. Subcellular location analysis showed that SGIV dUTPase is a cytoplasmic protein. Site-direct mutagenesis by overlap extension-PCR indicated that the NES is crucial for the translocation of SGIV dUTPase from the nucleus to the cytoplasm. We have discovered for the first time that the NES-dependent translocation of dUTPase is different for SGIV than for members of other species, which depend on a nuclear localization signal. These results provide new insights into the pathogenesis of fish iridoviruses.
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Authors | Jie Gong, You-Hua Huang, Xiao-Hong Huang, Rong Zhang, Qi-Wei Qin |
Journal | Archives of virology
(Arch Virol)
Vol. 155
Issue 7
Pg. 1069-76
(Jul 2010)
ISSN: 1432-8798 [Electronic] Austria |
PMID | 20461535
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Viral Proteins
- Pyrophosphatases
- dUTP pyrophosphatase
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Topics |
- Amino Acid Sequence
- Animals
- Cell Line
- Cloning, Molecular
- Computational Biology
- Fishes
- Gene Expression Profiling
- Gene Expression Regulation, Viral
(physiology)
- Iridovirus
(genetics, metabolism)
- Molecular Sequence Data
- Pyrophosphatases
(metabolism)
- Sequence Alignment
- Viral Proteins
(chemistry, genetics, metabolism)
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