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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1989-6-29
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pubmed:abstractText |
The RNA genome of tobacco etch virus (TEV) encodes a large polyprotein precursor that is processed to mature proteins by virus-specific proteinases. Cleavage sites located within the carboxyl-terminal two-thirds of the polyprotein are processed by a TEV-encoded 49 kd proteinase, while the enzyme(s) responsible for cleaving the remaining sites has not been found. In this study, a second TEV-encoded proteinase has been identified based on cell-free expression of defined RNA transcripts. The boundaries of this proteinase have been delineated by deletion analysis and site-directed mutagenesis. The proteolytically active domain has been localized to the carboxyl-terminal half of the 56 kd aphid-transmission helper component. A cleavage site that is recognized by this proteinase has been identified in the polyprotein adjacent to the carboxyl-terminus of the enzyme, and the proteinase appears to cleave by an autocatalytic mechanism. Proteolysis in vitro occurs between a Gly-Gly dipeptide as determined by radiochemical sequencing at the amino-terminus of the proteolytic product.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-16789265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-2842953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3001650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3009894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3011278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3031587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3039165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3041041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3186696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3277593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3282225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3285343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3286889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3409865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3467351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-3697076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-6091052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2656254-6384934
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
365-70
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:2656254-Amino Acid Sequence,
pubmed-meshheading:2656254-Binding Sites,
pubmed-meshheading:2656254-Endopeptidases,
pubmed-meshheading:2656254-Genes, Viral,
pubmed-meshheading:2656254-Molecular Sequence Data,
pubmed-meshheading:2656254-Mutation,
pubmed-meshheading:2656254-Plant Viruses,
pubmed-meshheading:2656254-Protein Precursors,
pubmed-meshheading:2656254-Protein Processing, Post-Translational
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pubmed:year |
1989
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pubmed:articleTitle |
A second proteinase encoded by a plant potyvirus genome.
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pubmed:affiliation |
Department of Biology, Texas A&M University, College Station 77843.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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