Linked Life Data

3285343

Source:http://linkedlifedata.com/resource/pubmed/id/3285343

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1988-6-22
pubmed:abstractText
Mature viral-encoded proteins of tobacco etch virus (TEV) arise by proteolytic processing of a large precursor. The proteinase responsible for most of these cleavages is a viral-encoded 49-kDa protein. All known or predicted cleavage sites in the TEV polyprotein are flanked by the conserved sequence motif Glu-Xaa-Xaa-Tyr-Xaa-Gln-Ser or Gly, with the scissile bond located between the Gln-Ser or Gly dipeptide. By using cell-free systems to manipulate and express cloned cDNA sequences, a 25-amino acid segment containing a putative proteolytic cleavage site of the TEV polyprotein has been introduced into the TEV capsid protein sequence. This recombinant protein is cleaved by the 49-kDa proteinase at the introduced cleavage site, thus demonstrating portability of a functional cleavage site. The role of the conserved amino acid sequence in determining substrate activity was tested by construction of engineered proteins that contained part or all of this motif. A protein that harbored an insertion of the conserved 7-amino acid segment was cleaved by the 49-kDa TEV proteinase. Cleavage of the synthetic precursor was shown to occur accurately between the expected Gln-Ser dipeptide by microsequence analysis. Proteins containing insertions that generated only the Gln-Ser, or only the serine moiety of the conserved sequence, were insensitive to the 49-kDa proteinase.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-16593574, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-16789257, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-16789265, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-3031587, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-3035560, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-3041039, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-3467351, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-3737407, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-4213287, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-4399049, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-5126466, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-5682314, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-6035483, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-6091052, http://linkedlifedata.com/resource/pubmed/commentcorrection/3285343-952885
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3391-5
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing.
pubmed:affiliation
Department of Microbiology, Oregon State University, Corvallis 97331.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.