Source:http://linkedlifedata.com/resource/pubmed/id/11172099
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Human immunodeficiency virus type 1 Gag and Gag-Pol precursors are translated from an mRNA which is indistinguishable from the full-length genomic RNA. The ratio of Gag to Gag-Pol polyproteins is approximately 20:1 and is controlled by a frameshift of the reading frame, which takes place downstream of the p7 nucleocapsid (NC) in the N terminus of the p1 peptide. The viral precursors Gag and Gag-Pol are cleaved by the virus-encoded protease (PR) into the structural proteins, and into p6(Pol), PR, reverse transcriptase and integrase. Due to the frameshift event, the cleavage site at the C terminus of NC coded in the Gag frame (ERQAN-FLGKI) changes either to ERQANFLRED or ERQANFFRED. The results presented in this report demonstrate that the NC released from the Gag-Pol precursor is 8 amino acid residues longer than the NC cleaved from the Gag polyprotein. Our results also show that truncated Gag-Pol precursors bearing cleavage site mutation at the NC/p6(Pol), and/or p6(Pol)/PR junctions, undergo autoprocessing in bacterial and eukaryotic cells, indicating that PR is active when part of the precursor.
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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/Gene Products, gag,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Protease,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gag Gene Products, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/p6 gag protein, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
581-90
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11172099-Animals,
pubmed-meshheading:11172099-Binding Sites,
pubmed-meshheading:11172099-COS Cells,
pubmed-meshheading:11172099-Cell Line,
pubmed-meshheading:11172099-Cercopithecus aethiops,
pubmed-meshheading:11172099-Enzyme Activation,
pubmed-meshheading:11172099-Gene Products, gag,
pubmed-meshheading:11172099-HIV Protease,
pubmed-meshheading:11172099-HIV-1,
pubmed-meshheading:11172099-Humans,
pubmed-meshheading:11172099-Nucleocapsid,
pubmed-meshheading:11172099-Protein Precursors,
pubmed-meshheading:11172099-Protein Processing, Post-Translational,
pubmed-meshheading:11172099-Recombinant Fusion Proteins,
pubmed-meshheading:11172099-Tumor Cells, Cultured,
pubmed-meshheading:11172099-gag Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2001
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pubmed:articleTitle |
Extended nucleocapsid protein is cleaved from the Gag-Pol precursor of human immunodeficiency virus type 1.
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pubmed:affiliation |
Experimental Pathology Unit and Clinical Virology Unit, The Hebrew University, Hadassah Medical School, PO Box 12272, Jerusalem 91120, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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