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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1994-7-13
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pubmed:databankReference | |
pubmed:abstractText |
The sequence of Rift Valley fever virus L segment that we published in a previous paper was erroneous in the 3'-terminal region of the antigenomic RNA molecule. Here, we have shown that the L segment is in fact 6404 nucleotides long and encodes a polypeptide of 237.7K in the viral complementary sense. Sequence comparisons performed between the RNA-dependent RNA polymerases of 22 negative-stranded RNA viruses revealed the existence of two novel regions located at the amino termini of the proteins and conserved only in the polymerases of bunya- and arenaviruses. In the region conserved in all RNA-dependent polymerases, corresponding to the so-called 'polymerase module', we identified a new motif, designated premotif A, common to all RNA-dependent polymerases, as well as amino acids located in the region between motifs preA and A which are strictly conserved for segmented negative-stranded RNA viruses. Using the recently released coordinates of human immunodeficiency virus reverse transcriptase and the alignment between all RNA-dependent polymerases in the 'polymerase module', we have determined the position of the conserved residues in these polymerases and discuss their possible functions in light of the available structural information.
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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/HIV Reverse Transcriptase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Replicase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Structural Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
75 ( Pt 6)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1345-52
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7515937-Amino Acid Sequence,
pubmed-meshheading:7515937-Arenavirus,
pubmed-meshheading:7515937-Cloning, Molecular,
pubmed-meshheading:7515937-Genes, Viral,
pubmed-meshheading:7515937-HIV Reverse Transcriptase,
pubmed-meshheading:7515937-Molecular Sequence Data,
pubmed-meshheading:7515937-Orthobunyavirus,
pubmed-meshheading:7515937-Protein Structure, Tertiary,
pubmed-meshheading:7515937-RNA, Viral,
pubmed-meshheading:7515937-RNA Replicase,
pubmed-meshheading:7515937-RNA-Directed DNA Polymerase,
pubmed-meshheading:7515937-Rift Valley fever virus,
pubmed-meshheading:7515937-Sequence Alignment,
pubmed-meshheading:7515937-Sequence Homology, Amino Acid,
pubmed-meshheading:7515937-Structure-Activity Relationship,
pubmed-meshheading:7515937-Viral Structural Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Rift Valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases.
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pubmed:affiliation |
Laboratoire des Bunyaviridés, CNRS URA 545, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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