PMID: 9557742Apr 29, 1998Paper

The rubella virus nonstructural protease requires divalent cations for activity and functions in trans

Journal of Virology
X LiuTeryl K Frey

Abstract

The rubella virus (RUB) nonstructural (NS) protease is a papain-like cysteine protease (PCP) located in the NS-protein open reading frame (NSP-ORF) that cleaves the NSP-ORF translation product at a single site to produce two products, P150 (the N-terminal product) and P90 (the C-terminal product). The RUB NS protease was found not to function following translation in vitro in a standard rabbit reticulocyte lysate system, although all of the other viral PCPs do so. However, in the presence of divalent cations such as Zn2+, Cd2+, and Co2+, the RUB NS protease functioned efficiently, indicating that these cations are required either as direct cofactors in catalytic activity or for correct acquisition of three-dimensional conformation of the protease. Since other viral and cell PCPs do not require cations for activity and the RUB NS protease contains a putative zinc binding motif, the latter possibility is more likely. Previous in vivo expression studies of the RUB NS protease failed to demonstrate trans cleavage activity (J.-P. Chen et al., J. Virol. 70:4707-4713, 1996). To study whether trans cleavage could be detected in vitro, a protease catalytic site mutant and a mutant in which the C-terminal 31 amino acids of P90 were delet...Continue Reading

Citations

Dec 21, 2012·The Journal of General Virology·Julia PerttiläTero Ahola
Aug 31, 1999·The Journal of General Virology·E ten DamM D Ryan
Feb 1, 2005·FEMS Immunology and Medical Microbiology·Umesh C Chaturvedi, Richa Shrivastava
Feb 11, 2020·Frontiers in Cellular and Infection Microbiology·Shweta SaraswatDeepak Sehgal
Oct 10, 2001·The Journal of Biological Chemistry·D ThibeaultA Pause

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