The substrate requirement for rubella virus protease trans -activity is unknown. Here, we analyzed the cleavability of RV P200-derived substrates varying in their N-terminal lengths (72–475 amino acids) from the cleavage site by the RV protease trans -activity. Only substrates with at least 309 amino acid residues N-terminal to the cleavage site were able to undergo cleavage. Further, rubella sequence was found to be necessary in the N-terminal region of the substrate, whereas a heterologous sequence C-terminal to the cleavage site was tolerated. These results demonstrated a requirement for residues located between amino acids 994–1102 of the RV P200 polyprotein, besides its cleavage site for RV protease trans -activity. This region overlaps with the starting site of the essential cis -protease activity of RV P200 polyprotein. This is a novel observation for a viral protease of the family Togaviridae .
Archives of Virology – Springer Journals
Published: Sep 1, 2006
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