About: Expression and partial purification of recombinant tomato ringspot nepovirus 3C-like proteinase: comparison of the activity of the mature proteinase and the VPg-proteinase precursor

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About: Expression and partial purification of recombinant tomato ringspot nepovirus 3C-like proteinase: comparison of the activity of the mature proteinase and the VPg-proteinase precursor Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Expression and partial purification of recombinant tomato ringspot nepovirus 3C-like proteinase: comparison of the activity of the mature proteinase and the VPg-proteinase precursor
Creator	Sanfaçon, Hélène Chisholm, Joan Wieczorek, Andrew
source	Elsevier; Medline; PMC
abstract	Abstract The 3C-like proteinase (Pro) from Tomato ringspot virus (genus Nepovirus) is responsible for the processing of the RNA1-encoded (P1) and RNA2-encoded (P2) polyproteins. Cleavage between the VPg and Pro domains is inefficient in vitro and in E. coli, resulting in the accumulation of the VPg-Pro. In this study, we have compared the trans-activity of the Pro and VPg-Pro on various P1- and P2-derived precursors. Recombinant Pro and VPg-Pro were partially purified using an E. coli expression system. A mutation of the VPg-Pro cleavage site was introduced into the VPg-Pro to prevent slow release of the Pro. The Pro was five to ten times more active than the VPg-Pro on two P2 cleavage sites (at the N- and C-termini of the movement protein domain) and was approximately two times more active than the VPg-Pro on the third P2 cleavage site (between the X3 and X4 domains). Neither the Pro nor the VPg-Pro could cleave in trans P1-derived substrates containing the three cleavage sites delineating the X1, X2, putative NTP-binding protein and VPg domains. These results are discussed in light of the possible regulation of the proteinase activity during virus replication.
has issue date	2001-11-05(xsd:dateTime)
bibo:doi	10.1016/s0168-1702(01)00344-6
bibo:pmid	11551656
has license	els-covid
sha1sum (hex)	976e1606a6c6059873ef793149db56adc5aa8993
schema:url	https://doi.org/10.1016/s0168-1702%2801%2900344-6
resource representing a document's title	Expression and partial purification of recombinant tomato ringspot nepovirus 3C-like proteinase: comparison of the activity of the mature proteinase and the VPg-proteinase precursor
has PubMed Central identifier	PMC7172257
has PubMed identifier	11551656
schema:publication	Virus Research
resource representing a document's body	covid:976e1606a6c6059873ef793149db56adc5aa8993#body_text
is schema:about of	named entity 'mutation' named entity 'Pro' named entity 'VPg' named entity 'processing' named entity 'proteinase' »more»

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