Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease

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DOIResolve DOI: http://doi.org/10.1016/j.abb.2007.07.006
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TypeArticle
Journal titleArchives of Biochemistry and Biophysics
Volume466
Issue1
Pages814; # of pages: 7
AbstractThe severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) carries out N-terminal processing of the viral replicase polyprotein, and also exhibits Lys48-linked polyubiquitin chain debranching and ISG15 precursor processing activities in vitro. Here, we used SDS–PAGE and fluorescence-based assays to demonstrate that ISG15 derivatives are the preferred substrates for the deubiquitinating activity of the PLpro. With kcat/KM of 602,000 M−1 s−1, PLpro hydrolyzes ISG15-AMC 30- and 60-fold more efficiently than Ub-AMC and Nedd8-AMC, respectively. Data obtained with truncated ISG15 and hybrid Ub/ISG15 substrates indicate that both the N- and C-terminal Ub-like domains of ISG15 contribute to this preference. The enzyme also displays a preference for debranching Lys48- over Lys63-linked polyubiquitin chains. Our results demonstrate that SARS-CoV PLpro can differentiate between ubiquitin-like modifiers sharing a common C-terminal sequence, and that the debranching activity of the PLpro is linkage type selective. The potential structural basis for the demonstrated specificity of SARS-CoV PLpro is discussed.
Publication date
AffiliationNational Research Council Canada; NRC Biotechnology Research Institute
Peer reviewedNo
NPARC number12327845
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Record identifierf9213884-93b2-4fab-af64-932a720769c7
Record created2009-09-10
Record modified2016-05-09
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