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KMID : 1234420090370030287
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Korean Journal of Microbiololgy and Biotechnology
2009 Volume.37 No. 3 p.287 ~ p.292
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Functional Characterization of Phosphorylation of the Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) Nucleocapsid Protein
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Lee Chang-Hee
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Abstract
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The nucleocapsid (N) protein of porcine reproductive and respiratory syndrome virus (PRRSV) is a basic multifunctional
protein which has been reported to be a serine phosphoprotein with yet-identified functions. As a first step towards understanding the general role of N protein phosphorylation during virus replication, the non-phosphorylated mutant N gene was constructed by mutating all serine residues to alanine. This recombinant N protein was identified to be unphosphorylated, confirming that serine residues truly function as core amino acids responsible for N protein phosphorylation. The PRRSV N protein has been shown to possess the biological features of nuclear localization and N-N homodimerization which individually play critical roles in virus infection. In the present study, therefore, it was attempted to investigate whether these two properties of the N protein are modulated by its phosphorylation status. However, experimental results showed that the nonphosphorylated N protein was still present in the nucleus and nucleolus, and was able to associate with itself by non-covalent interactions. Taken together, the data suggest phosphorylation-independent regulation of N protein nuclear transport or oligomerization, thereby implying the potential involvement of phosphorylation in regulating the activities of the N protein at other levels including RNA-binding capacity.
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KEYWORD
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PRRSV, nucleocapsid protein, serine phosphoprotein, nuclear localization, homodimerization
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