The endopeptidase of the maize-affecting Marafivirus type member maize rayado fino virus doubles as a deubiquitinase
| Autor: | Ankoor Patel, Brian L. Mark, Jessica A.M. McBride |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
RNA viruses Marafivirus viruses MRFV TYMV PRO papain-like cysteine protease of TYMV medicine.disease_cause Virus Replication 01 natural sciences Biochemistry Tymoviridae Deubiquitinating enzyme Ubiquitin structural biology maize rayado fino virus Ub ubiquitin ASU asymmetric unit CSDaV citrus sudden death–associated virus 0303 health sciences biology PROs proteases DUB deubiquitinase +ssRNA positive-sense ssRNA Cell biology polyprotein TYMV turnip yellow mosaic virus BlVS blackberry virus S MR molecular replacement MRFV maize rayado fino virus Research Article Proteases Polyproteins food.ingredient Viral protein RNA-dependent RNA polymerase papain-like protease Genome Viral ubiquitin hydrolase Zea mays OTUD3 ovarian tumor domain–containing protein 3 03 medical and health sciences food OLV3 Olive latent virus 3 Endopeptidases ubiquitin medicine RdRp RNA-dependent RNA polymerase AMC 7-amino-4-methylcoumarin Molecular Biology 030304 developmental biology Virus Assembly CSS complex formation significance score Cell Biology CP coat protein GSyV1 Grapevine Syrah virus 1 deubiquitinase Viral replication biology.protein HEL helicase Ub-3Br ubiquitin(1–75)–3-bromopropylamine 010606 plant biology & botany OBDV oat blue dwarf virus |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 1083-351X |
| Popis: | Marafiviruses are capable of persistent infection in a range of plants that have importance to the agriculture and biofuel industries. Although the genomes of a few of these viruses have been studied in-depth, the composition and processing of the polyproteins produced from their main ORFs have not. The Marafivirus polyprotein consists of essential proteins that form the viral replicase, as well as structural proteins for virus assembly. It has been proposed that Marafiviruses code for cysteine proteases within their polyproteins, which act as endopeptidases to autocatalytically cleave the polyprotein into functional domains. Furthermore, it has also been suggested that Marafivirus endopeptidases may have deubiquitinating activity, which has been shown to enhance viral replication by downregulating viral protein degradation by the ubiquitin (Ub) proteasomal pathway as well as tampering with cell signaling associated with innate antiviral responses in other positive-sense ssRNA viruses. Here, we provide the first evidence of cysteine proteases from six different Marafiviruses that harbor deubiquitinating activity and reveal intragenus differences toward Ub linkage types. We also examine the structural basis of the endopeptidase/deubiquitinase from the Marafivirus type member, maize rayado fino virus. Structures of the enzyme alone and bound to Ub reveal marked structural rearrangements that occur upon binding of Ub and provide insights into substrate specificity and differences that set it apart from other viral cysteine proteases. |
| Databáze: | OpenAIRE |
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