Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/66667
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dc.contributor.authorHuang, Y.J.en_US
dc.contributor.author黃千衿zh_TW
dc.contributor.authorChien, M.S.en_US
dc.contributor.authorWu, C.Y.en_US
dc.contributor.authorHuang, C.J.en_US
dc.contributor.author簡茂盛zh_TW
dc.date2005zh_TW
dc.date.accessioned2014-06-11T05:46:57Z-
dc.date.available2014-06-11T05:46:57Z-
dc.identifier.issn0166-0934zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/66667-
dc.description.abstractPseudorabies virus (PRV) is an alphaherpesvirus, and its gene organization and regulation are similar to the well-characterized human herpes simplex virus (HSV). The PRV early protein UL54 consists of 363 amino acids with homology to the HSV ICP27 immediate-early protein. Previously, we have demonstrated the nuclear accumulation and poly(G) RNA-binding activity of UL54 protein. In the present study, we have identified further the functional regions within UL54 conferring for nuclear localization and RNA-binding activity. Several recombinant expression plasmids containing various coding regions of UL54 gene were constructed for producing a series of C-terminally truncated or internally deleted forms of UL54 mutants in Escherichia coli or porcine kidney (PK-15) cells. RNA-binding activity of E. coli-expressed UL54 mutants was characterized by the binding ability to poly(G) RNA homopolymer in dot blot hybridization assay and the results have shown that the N-terminal 83 residues were responsible for RNA-binding, and the region of residues 35-82 containing an RGG box was necessary for its function. Furthermore, the region responsible for nuclear localization was investigated by transient expression of various deletion mutants in PK-15 cells followed by detection of their subcellular distribution. The results showed that C-terminal deletion beyond the amino acid residue 83 or internal deletion containing the RGG box sequence could restrict UL54 mutants in the cytoplasm. The ability of the N-terminal 83 residues to target the green fluorescence protein to the nucleus confirmed further its role as a functional nuclear localization signal (NLS). The utmost N-terminal 83 residues portion of UL54 contains two important functional domains, NLS and RNA-binding, and thus it would play an indispensable role in UL54 regulatory function. (c) 2005 Elsevier B.V. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Virological Methodsen_US
dc.relation.ispartofseriesJournal of Virological Methods, Volume 130, Issue 1-2, Page(s) 102-107.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.jviromet.2005.06.011en_US
dc.subjectimmediate-early proteinen_US
dc.subjectregulatory proteinen_US
dc.subjectgene-expressionen_US
dc.subjecticp27en_US
dc.subjecttranscriptionen_US
dc.subjectinfectionen_US
dc.subjectdomainsen_US
dc.subjectsignalen_US
dc.titleMapping of functional regions conferring nuclear localization and RNA-binding activity of pseudorabies virus early protein UL54en_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.jviromet.2005.06.011zh_TW
item.languageiso639-1en_US-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.openairetypeJournal Article-
Appears in Collections:微生物暨公共衛生學研究所
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