Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.
AUTOR(ES)
Ahn, B Y
RESUMO
Glutaredoxins (GRXs), also known as thioltransferases, use glutathione as a cofactor for reduction of disulfides in prokaryotes and eukaryotes. We demonstrate that the vaccinia virus O2L open reading frame encodes a functional GRX, as predicted by Johnson et al. [Johnson, G. P., Goebel, S. J., Perkus, M. E., Davis, S. W., Winslow, J. P. & Paoletti, E. (1991) Virology 181, 378-381] from sequence homology. The 12-kDa protein product of the O2L open reading frame was synthesized after viral DNA replication, coincident with a major increase in cytoplasmic glutathione-dependent thioltransferase activity. The protein was associated with purified vaccinia virions and was not released by treatment with a nonionic detergent unless dithiothreitol was added. The virion-derived protein, as well as a recombinant form expressed in Escherichia coli, exhibited thioltransferase and dehydroascorbate reductase activities indicative of a functional GRX. The postreplicative synthesis of vaccinia virus GRX and its association with virions suggest that the enzyme may have novel roles in the virus growth cycle.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=49645Documentos Relacionados
- Human immunodeficiency virus vpr product is a virion-associated regulatory protein.
- Methylation of messenger RNA of Newcastle disease virus in vitro by a virion-associated enzyme.
- Cauliflower mosaic virus coat protein is phosphorylated in vitro by a virion-associated protein kinase
- Methyl group analysis of virion-associated high-molecular-weight RNA synthesized in vitro by purified vaccinia virus.
- Cell-free translation of purified virion-associated high-molecular-weight RNA synthesized in vitro by vaccinia virus.