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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0035924,
umls-concept:C0042776,
umls-concept:C0178827,
umls-concept:C0205245,
umls-concept:C0559956,
umls-concept:C1136102,
umls-concept:C1418578,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
8
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pubmed:dateCreated |
2009-3-19
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pubmed:abstractText |
The rubella virus (RUBV) capsid (C) protein rescues mutants with a lethal deletion between two in-frame NotI sites in the P150 replicase gene, a deletion encompassing nucleotides 1685 to 2192 of the RUBV genome and amino acids (aa) 548 to 717 of P150 (which has a total length of 1,301 aa). The complete domain rescuable by the C protein was mapped to aa 497 to 803 of P150. Introduction of aa 1 to 277 of the C protein (lacking the C-terminal E2 signal sequence) between the NotI sites in the P150 gene in a replicon construct yielded a viable construct that synthesized viral RNA with wild-type kinetics, indicating that C and this region of P150 share a common function. Further genetic analysis revealed that an arginine-rich motif between aa 60 and 68 of the C protein was necessary for the rescue of DeltaNotI deletion mutants and substituted for an arginine-rich motif between aa 731 and 735 of the P150 protein when the C protein was introduced into P150. Possible common functions shared by these arginine-rich motifs include RNA binding and interaction with cell proteins.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-10823864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-11520607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-11601918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-11884543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-12034482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-12915564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15047844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15141033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15183337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-1518855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15298168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15827189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15846844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-15907967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16051872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16078876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16271890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16428606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16571813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16775315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16971445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-16979208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-17037511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-17660191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-18305028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-18987156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-7531822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-7817880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19176617-8026476
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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 |
Apr
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pubmed:issn |
1098-5514
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3549-55
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19176617-Capsid Proteins,
pubmed-meshheading:19176617-Mutagenesis, Insertional,
pubmed-meshheading:19176617-Protein Structure, Tertiary,
pubmed-meshheading:19176617-RNA Replicase,
pubmed-meshheading:19176617-Recombination, Genetic,
pubmed-meshheading:19176617-Rubella virus,
pubmed-meshheading:19176617-Sequence Deletion,
pubmed-meshheading:19176617-Virus Replication
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pubmed:year |
2009
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pubmed:articleTitle |
Functional replacement of a domain in the rubella virus p150 replicase protein by the virus capsid protein.
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pubmed:affiliation |
Biology Department, Georgia State University, P.O. Box 4010, Atlanta, GA 30302-4010, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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