Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1997-4-21
|
pubmed:abstractText |
The tobacco etch potyvirus (TEV) helper component-proteinase (HC-Pro, 460 amino acid residues) is a multifunctional protein involved in aphid-mediated transmission, genome amplification, polyprotein processing, and long-distance movement. To investigate the interrelationships between three of these functions, 25 alanine-scanning mutations affecting clusters of charged residues were introduced into the HC-Pro coding sequence. The resulting mutants were analyzed with respect to HC-Pro proteolytic activity in vitro, genome amplification in protoplasts, and long-distance movement in tobacco plants. Three classes of mutants were identified. Class I mutants (total of 17) were capable of genome amplification, long-distance movement, and HC-Pro proteolysis with efficiencies similar to parental virus. The class III mutant (total of 1) encoded a proteolytically debilitated HC-Pro and was replication-defective. Class II mutants (total of 7) encoded proteolytically active HC-Pro, but each exhibited a suppressed amplification phenotype that was characterized by a progressive shutoff during the course of infection in protoplasts. The class II mutants also exhibited defects in long-distance movement, accumulating to relative levels of 0 to 7.5% in noninoculated tissue. Wild-type HC-Pro supplied in trans was able to partially rescue the class II mutant amplification defects in protoplasts and long-distance movement defects in plants, although the extent of complementation of movement function varied for each mutant. Six of the seven class II mutations affected the central region of HC-Pro between residues 126 and 300, whereas only one affected the C-terminal proteolytic domain. These results indicate that the central region of HC-Pro is necessary for efficient genome amplification and long-distance movement, and that the one or more HC-Pro functions involved in these processes is at least partially trans-active. Additionally, the long-distance movement properties of a previously characterized HC-Pro-defective mutant (TEV-GUS/CCCE) were characterized further using grafted nontransgenic and HC-Pro-expressing transgenic plants. The results indicated that HC-Pro is required in both inoculated and noninoculated tissues to complement the TEV-GUS/CCCE movement defects.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0042-6822
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
228
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
251-62
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:9123832-Alanine,
pubmed-meshheading:9123832-Binding Sites,
pubmed-meshheading:9123832-Cysteine Endopeptidases,
pubmed-meshheading:9123832-Gene Amplification,
pubmed-meshheading:9123832-Genetic Complementation Test,
pubmed-meshheading:9123832-Genome, Viral,
pubmed-meshheading:9123832-Movement,
pubmed-meshheading:9123832-Mutagenesis,
pubmed-meshheading:9123832-Plants, Genetically Modified,
pubmed-meshheading:9123832-Plants, Toxic,
pubmed-meshheading:9123832-Potyvirus,
pubmed-meshheading:9123832-Protein Processing, Post-Translational,
pubmed-meshheading:9123832-Protoplasts,
pubmed-meshheading:9123832-Tobacco,
pubmed-meshheading:9123832-Viral Proteins
|
pubmed:year |
1997
|
pubmed:articleTitle |
Genome amplification and long-distance movement functions associated with the central domain of tobacco etch potyvirus helper component-proteinase.
|
pubmed:affiliation |
Department of Biology, Texas A&M University, College Station 77843, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|