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Título: | Gemin5 proteolysis reveals a novel motif to identify L protease targets |
Autor: | Piñeiro, David; Ramajo, Jorge CSIC; Bradrick, Shelton S.; Martínez-Salas, Encarnación CSIC ORCID | Fecha de publicación: | 2012 | Editor: | Oxford University Press | Citación: | Nucleic Acids Research 40: 4942- 4953 (2012) | Resumen: | Translation of picornavirus RNA is governed by the internal ribosome entry site (IRES) element, directing the synthesis of a single polyprotein. Processing of the polyprotein is performed by viral proteases that also recognize as substrates host factors. Among these substrates are translation initiation factors and RNA-binding proteins whose cleavage is responsible for inactivation of cellular gene expression. Foot-and-mouth disease virus (FMDV) encodes two proteases, L pro and 3C pro. Widespread definition of L pro targets suffers from the lack of a sufficient number of characterized substrates. Here, we report the proteolysis of the IRES-binding protein Gemin5 in FMDV-infected cells, but not in cells infected by other picornaviruses. Proteolysis was specifically associated with expression of L pro, yielding two stable products, p85 and p57. In silico search of putative L targets within Gemin5 identified two sequences whose potential recognition was in agreement with proteolysis products observed in infected cells. Mutational analysis revealed a novel L pro target sequence that included the RKAR motif. Confirming this result, the Fas-ligand Daxx, was proteolysed in FMDV-infected and L pro-expressing cells. This protein carries a RRLR motif whose substitution to EELR abrogated L pro recognition. Thus, the sequence (R)(R/K)(L/A)(R) defines a novel motif to identify putative targets of L pro in host factors. | URI: | http://hdl.handle.net/10261/115725 | DOI: | 10.1093/nar/gks172 | Identificadores: | doi: 10.1093/nar/gks172 issn: 0305-1048 |
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