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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2005-5-13
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pubmed:abstractText |
The arenavirus L protein has the characteristic sequence motifs conserved among the RNA-dependent RNA polymerase L proteins of negative-strand (NS) RNA viruses. Studies based on the use of reverse-genetics approaches have provided direct experimental evidence of the key role played by the arenavirus L protein in viral-RNA synthesis. Sequence alignment shows six conserved domains among L proteins of NS RNA viruses. The proposed polymerase module of L is located within its domain III, which contains highly conserved amino acids within motifs designated A and C. We have examined the role of these conserved residues in the polymerase activity of the L protein of the prototypic arenavirus, lymphocytic choriomeningitis virus (LCMV), in vivo using a minigenome rescue assay. We show here that the presence of sequence SDD, a characteristic of motif C of segmented NS RNA viruses, as well as the presence of the highly conserved D residue within motif A of L proteins, is strictly required for the polymerase activity of the LCMV L protein. The strong dominant negative phenotype associated with many of the mutants examined and results from coimmunoprecipitation studies provided genetic and biochemical evidence, respectively, for the requirement of the L-L interaction for the polymerase activity of the LCMV L protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-10502516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-10504728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-10557268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-10708446,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11080486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11119613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11208257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11437666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11533204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11677245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11711615,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-11988060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-12490411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-12504565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-12584310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-12808132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-1402814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-14563923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-14972544,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-1626415,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-2705303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-7491760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-7706217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-7815484,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9224928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9420283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9526012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9557665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9851928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15890965-9878607
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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 |
Jun
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7262-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15890965-Amino Acid Motifs,
pubmed-meshheading:15890965-Amino Acid Substitution,
pubmed-meshheading:15890965-Animals,
pubmed-meshheading:15890965-Cell Line,
pubmed-meshheading:15890965-Conserved Sequence,
pubmed-meshheading:15890965-Cricetinae,
pubmed-meshheading:15890965-Genes, Viral,
pubmed-meshheading:15890965-Lymphocytic choriomeningitis virus,
pubmed-meshheading:15890965-Mutagenesis, Site-Directed,
pubmed-meshheading:15890965-Protein Structure, Quaternary,
pubmed-meshheading:15890965-RNA, Viral,
pubmed-meshheading:15890965-RNA Replicase,
pubmed-meshheading:15890965-Recombinant Proteins,
pubmed-meshheading:15890965-Viral Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Genetic and biochemical evidence for an oligomeric structure of the functional L polymerase of the prototypic arenavirus lymphocytic choriomeningitis virus.
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pubmed:affiliation |
Department of Neuropharmacology IMM-6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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