Document Type
Thesis - University Access Only
Award Date
2000
Degree Name
Master of Science (MS)
Department / School
Biology and Microbiology
Abstract
The nucleocapsid (N) protein of porcine reproductive and respiratory syndrome virus is a 123 amino acid structural protein required for packaging the single stranded RNA genome. In addition to its structural function, we propose that the N protein is also involved in regulation of host cell function during replication. Using enhanced green fluorescent protein as a tag, we identified a highly conserved basic region (residues 43- 60) which is required for N protein nucleolar localization and is capable of directing the nuclear and nucleolar translocation of an otherwise cytoplasmic protein, ~ - galactosidase. Mutation analysis showed that the basic residues Lysine 43 and Lysine 44 are critical for nucleolar targeting of the N protein. N protein nuclear import was enhanced by modifying the phosphorylation of two CK-II sites (threonine 59 and threonine 68). These results demonstrate that N protein contains a functional nucleolar localization signal sequence (residues 43-60) which directs N protein to the cell nucleolus and suggest that CK-II phosphorylation plays a role in the regulation of N protein nucleolar localization.
Library of Congress Subject Headings
Swine -- Virus diseases
Nucleoproteins
Porcine reproductive and respiratory syndrome
Number of Pages
55
Recommended Citation
Fang, Ying, "Characterization of a Nucleolar Localization Signal Motif in Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Protein" (2000). Electronic Theses and Dissertations. 745.
https://openprairie.sdstate.edu/etd2/745