Source:http://linkedlifedata.com/resource/pubmed/id/10814574
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-6-30
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pubmed:abstractText |
Tobacco mosaic virus produces two proteins that contain domains similar to the methyltransferase (MT) and helicase (HEL)-like domains of the replicase-associated proteins of other RNA viruses. The more abundant 126-kDa protein contains only the MT and HEL-like domains, whereas the 183-kDa readthrough protein additionally contains the polymerase domain. We examined the functions of these proteins by constructing a bipartite system to express the 126- and 183-kDa proteins from separate RNAs. Mutants expressing the 183-kDa protein recognized promoters for negative- and positive-stranded RNA synthesis, transcribed subgenomic mRNAs, capped RNAs, synthesized proteins, moved cell to cell within the plant, and replicated defective RNAs (dRNAs). The principal function of the 126-kDa protein was to increase the rate of replication approximately tenfold. The 126-kDa protein appeared to function primarily in cis, and production of the 126-kDa protein in trans did not enhance replication of the helper virus. dRNAs producing a functional 126-kDa protein were replicated efficiently by helper viruses that produced only the 183-kDa protein but not by wild-type virus, suggesting that efficient replication required the 183-kDa protein to form a heterodimer with the 126-kDa protein already bound to the target dRNA.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/130k protein, Tobacco mosaic virus,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Viral Movement Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Replicase,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tobacco mosaic virus replicase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10814574-Frameshift Mutation,
pubmed-meshheading:10814574-Gene Expression Regulation, Viral,
pubmed-meshheading:10814574-Molecular Weight,
pubmed-meshheading:10814574-Plant Viral Movement Proteins,
pubmed-meshheading:10814574-Plants, Toxic,
pubmed-meshheading:10814574-RNA Replicase,
pubmed-meshheading:10814574-Tobacco,
pubmed-meshheading:10814574-Tobacco Mosaic Virus,
pubmed-meshheading:10814574-Viral Proteins,
pubmed-meshheading:10814574-Virus Replication
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pubmed:year |
2000
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pubmed:articleTitle |
Functions of the 126- and 183-kDa proteins of tobacco mosaic virus.
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pubmed:affiliation |
Department of Plant Pathology, University of Florida, Citrus Research and Education Center, 700 Experiment Station Road, Lake Alfred, Florida 33850, USA. djlew@lal.ufl.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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