About: The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity

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About: The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity
Creator	Chen, H Atreya, C Stark, C
source	PMC
abstract	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.
has issue date	2006-03-27(xsd:dateTime)
bibo:doi	10.1007/s00705-006-0744-9
bibo:pmid	16570206
has license	no-cc
sha1sum (hex)	7b242f0ac81dd1f79d0c471df13f90426b0383bd
schema:url	https://doi.org/10.1007/s00705-006-0744-9
resource representing a document's title	The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity
has PubMed Central identifier	PMC7086818
has PubMed identifier	16570206
schema:publication	Arch Virol
resource representing a document's body	covid:7b242f0ac81dd1f79d0c471df13f90426b0383bd#body_text
is schema:about of	named entity 'INTERNAL' named entity 'amino acid' named entity 'family' named entity 'NOVEL' named entity '994' »more»

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