๐ Characterization of the nuclear export signal in the coronavirus infections bronchitis virus nucleocapsid protein
The nucleocapsid (N) protein of infectious bronchitis virus (IBV) localizes to the cytoplasm and nucleolus and contains an eight-amino-acid nucleolar retention motif. In this study, a leucine-rich nuclear export signal (NES) (291-LQLDGLHL-298) present in the C-terminal region of the IBV N protein was analyzed by using alanine substitution and deletion mutagenesis to investigate the relative contributions that leucine residues make to nuclear export and where these residues are located on the structure of the IBV N protein. The analysis indicated that Leu296 and Leu298 are required for efficient nuclear export of the proiein. Structural information indicated that both of these amino acids are available for interaction with protein complexes involved in this process. However, export of N protein from the nucleus/nucleolus was not inhibited by leptomycin B treatment, indicating that N protein nuclear export is independent of the CRM1-mediated export pathway. Copyright ยฉ 2007, American Society for Microbiology.
keywords
๐ bronchitis virus (233)
๐ amino acid (454)
๐ infectious bronchitis (235)
๐ amino acids (205)
author
๐ค Reed, Mark L.
๐ค Howell, Gareth
๐ค Harrison, Sally M.
๐ค Spencer, Kelly Anne
๐ค Hiscox, Julian A.
year
โฐ 2007
journal
๐ Journal of Virology
issn
๐ 0022538X
volume
81
number
8
page
4298-4304
citedbycount
15
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