Structural highlights
Publication Abstract from PubMed
The Baculoviridae family of viruses encode a viral Ubiquitin gene. Though the viral Ubiquitin (vUb) is homologous to the host eukaryotic Ubiquitin (Ub), its preservation in the viral genome indicates unique functions that are not compensated by the host Ub. We report the structural, biophysical, and biochemical properties of the vUb from Autographa Californica Multiple Nucleo-Polyhedrosis Virus (AcMNPV). The packing of central helix alpha1 to the beta-sheet b1-b5 is different between vUb and Ub. Consequently, its stability is lower compared to Ub. However, the surface properties, ubiquitination activity, and the interaction with Ubiquitin binding domains are similar between vUb and Ub. Interestingly, vUb forms atypical polyubiquitin chain linked by lysine at the 54th position (K54), and the deubiquitinating enzymes are ineffective against the K54-linked polyubiquitin chains. We propose that the modification of host/viral proteins with the K54-linked chains is an effective way selected by the virus to protect the vUb signal from host DUBs.
-A novel polyubiquitin chain linkage formed by viral Ubiquitin is resistant to host deubiquitinating enzymes.,Negi H, Reddy PP, Vengayil V, Patole C, Laxman S, Das R Biochem J. 2020 Jun 1. pii: 225104. doi: 10.1042/BCJ20200289. PMID:32478812[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Negi H, Reddy PP, Vengayil V, Patole C, Laxman S, Das R. -A novel polyubiquitin chain linkage formed by viral Ubiquitin is resistant to host deubiquitinating enzymes. Biochem J. 2020 Jun 1. pii: 225104. doi: 10.1042/BCJ20200289. PMID:32478812 doi:http://dx.doi.org/10.1042/BCJ20200289
