id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-004738-vnz15x84	Chen, H. H.	The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity	2006-03-27		.txt	text/plain	3966	160	52	To evaluate the trans-cleavage activity of RV protease on P200-derived substrates, a series of RV P200-related polypeptide expression plasmids that express protein with different N-terminal lengths from the cleavage site (72, 199, 309, and 475 residues) were constructed. To test whether replacement of P200-related sequences C-terminal to the cleavage site by non-rubella sequences affect RV protease trans-activity, the plasmid pRVS-GFP, which contains PCR-amplified RV protease substrate sequences representing polypeptide residues 827-1306 (residues 1302-1306 represent the C-terminal side of the cleavage site), fused at its C-terminus to GFP ORF in-frame, was created (Fig. 1B) . Similarly, to test whether a heterologous sequence on the N-terminal side of the cleavage site affects substrate recognition by the protease trans-activity, GFP ORF was fused in-frame at the N-terminus of the rubella sequence in the plasmid pRVS-1102-1548 to create pRVS-GFP-1102-1548 (Fig. 1B) . In this report, we have shown that RV protease trans-activity demonstrates substrate specificity by requiring an internal sequence within the region that is N-terminal to the cleavage site.	./cache/cord-004738-vnz15x84.txt	./txt/cord-004738-vnz15x84.txt