Please use this identifier to cite or link to this item: https://doi.org/10.1111/j.1742-4658.2007.05947.x
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dc.titleExpression, post-translational modification and biochemical characterization of proteins encoded by subgenomic mRNA8 of the severe acute respiratory syndrome coronavirus
dc.contributor.authorLe, T.M.
dc.contributor.authorWong, H.H.
dc.contributor.authorTay, F.P.L.
dc.contributor.authorFang, S.
dc.contributor.authorKeng, C.-T.
dc.contributor.authorTan, Y.J.
dc.contributor.authorLiu, D.X.
dc.date.accessioned2014-10-27T08:28:11Z
dc.date.available2014-10-27T08:28:11Z
dc.date.issued2007-08
dc.identifier.citationLe, T.M., Wong, H.H., Tay, F.P.L., Fang, S., Keng, C.-T., Tan, Y.J., Liu, D.X. (2007-08). Expression, post-translational modification and biochemical characterization of proteins encoded by subgenomic mRNA8 of the severe acute respiratory syndrome coronavirus. FEBS Journal 274 (16) : 4211-4222. ScholarBank@NUS Repository. https://doi.org/10.1111/j.1742-4658.2007.05947.x
dc.identifier.issn1742464X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100650
dc.description.abstractThe most striking difference between the subgenomic mRNA8 of severe acute respiratory syndrome coronavirus isolated from human and some animal species is the deletion of 29 nucleotides, resulting in splitting of a single ORF (ORF8) into two ORFs (ORF8a and ORF8b). ORF8a and ORF8b are predicted to encode two small proteins, 8a and 8b, and ORF8 a single protein, 8ab (a fusion form of 8a and 8b). To understand the functions of these proteins, we cloned cDNA fragments covering these ORFs into expression plasmids, and expressed the constructs in both in vitro and in vivo systems. Expression of a construct containing ORF8a and ORF8b generated only a single protein, 8a; no 8b protein expression was obtained. Expression of a construct containing ORF8 generated the 8ab fusion protein. Site-directed mutagenesis and enzymatic treatment revealed that protein 8ab is modified by N-linked glycosylation on the N81 residue and by ubiquitination. In the absence of the 8a region, protein 8b undergoes rapid degradation by proteasomes, and addition of proteasome inhibitors inhibits the degradation of protein 8b as well as the protein 8b-induced rapid degradation of the severe acute respiratory syndrome coronavirus E protein. Glycosylation could also stabilize protein 8ab. More interestingly, the two proteins could bind to monoubiquitin and polyubiquitin, suggesting the potential involvement of these proteins in the pathogenesis of severe acute respiratory syndrome coronavirus. © 2007 The Authors.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1111/j.1742-4658.2007.05947.x
dc.sourceScopus
dc.subjectGlycosylation
dc.subjectmRNA8
dc.subjectRapid degradation
dc.subjectSARS-CoV
dc.subjectUbiquitination
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1111/j.1742-4658.2007.05947.x
dc.description.sourcetitleFEBS Journal
dc.description.volume274
dc.description.issue16
dc.description.page4211-4222
dc.identifier.isiut000249010400017
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