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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2002-2-11
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pubmed:abstractText |
The herpes simplex virus type 1 gamma(1)34.5 gene product precludes the host-mediated protein shutoff response induced by activated protein kinase R (PKR). Earlier studies demonstrated that recombinant viruses lacking the gamma(1)34.5 gene (Deltagamma(1)34.5) developed secondary mutations that allowed earlier U(S)11 expression and enabled continued protein synthesis. Further, in vitro studies demonstrated that a recombinant expressed U(S)11 protein binds PKR, blocks the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) by activated PKR, and, if provided prior to PKR activation, precluded PKR autophosphorylation. The present study furthers the hypothesis that early U(S)11 production precludes PKR-mediated host protein shutoff by demonstrating that (i) U(S)11 and PKR interact in the context of viral infection, (ii) this interaction is RNA dependent and requires a 30-amino-acid domain (amino acids 91 to 121) in the carboxyl domain of the U(S)11 protein, (iii) the proteins biochemically colocalize in the S100 ribosomal fraction, and (iv) there is a PKR substrate domain immediately adjacent to the binding domain. The results suggest that the U(S)11 interaction with PKR at the ribosome is RNA dependent and that the U(S)11 protein contains a substrate domain with homology to eIF-2alpha in close proximity to an essential binding domain.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-10074192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-11070019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-11333900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-1314384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-1316472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-1375230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-163344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-163916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-1656075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-1920611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-2173860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-4300104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-6173662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-6871224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-7537157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-7678306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8094759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8099586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8202476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8383175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8525619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8627758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8663319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-8887567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-9023344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-9079663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-9223497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-9696792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11836380-9765401
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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 |
Mar
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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 |
76
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2029-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11836380-Amino Acid Sequence,
pubmed-meshheading:11836380-Animals,
pubmed-meshheading:11836380-Binding Sites,
pubmed-meshheading:11836380-Cell Line,
pubmed-meshheading:11836380-Herpes Simplex,
pubmed-meshheading:11836380-Herpesvirus 1, Human,
pubmed-meshheading:11836380-Humans,
pubmed-meshheading:11836380-Molecular Sequence Data,
pubmed-meshheading:11836380-Phosphorylation,
pubmed-meshheading:11836380-RNA-Binding Proteins,
pubmed-meshheading:11836380-Rabbits,
pubmed-meshheading:11836380-Ribosomal Proteins,
pubmed-meshheading:11836380-Viral Proteins,
pubmed-meshheading:11836380-eIF-2 Kinase
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pubmed:year |
2002
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pubmed:articleTitle |
The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain.
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pubmed:affiliation |
Department of Pediatrics, The University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL 35294, USA. kcassady@peds.uab.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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