Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-10-20
pubmed:databankReference
pubmed:abstractText
The cDNA for a human homologue (hIF2) of bacterial (bIF2) and yeast (yIF2) translation initiation factor two (IF2) has been identified during a screen for proteins which interact with HIV-1 matrix. The hIF2 cDNA encodes a 1220-amino-acid protein with a predicted relative molecular mass of 139 kDa, though endogeneous hIF2 migrates anomalously on SDS/PAGE at 180 kDa. hIF2 has an extended N-terminus compared with its homologues, although its central GTP-binding domain and C-terminus are highly conserved, with 58% sequence identity with yIF2. We have confirmed that hIF2 is required for general translation in human cells by generation of a point mutation in the P-loop of the GTP-binding domain. This mutant protein behaves in a transdominant manner in transient transfections and leads to a significant decrease in the translation of a reporter gene. hIF2 interacts directly with HIV-1 matrix and Gag in vitro, and the protein complex can be immunoprecipitated from human cells. This interaction appears to block hIF2 function, since purified matrix protein inhibits translation in a reticulocyte lysate. hIF2 does not correspond to any of the previously characterized translation initiation factors identified in mammals, but its essential role in translation appears to have been conserved from bacteria to humans.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-1112800, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-1620067, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-1830345, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-2200518, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-57617, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8065455, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8076820, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8107229, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8139035, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8344494, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8608135, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8882578, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8985244, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-8999877, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9151848, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9445076, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9562972, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9624054, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9671805, http://linkedlifedata.com/resource/pubmed/commentcorrection/10432305-9720861
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
342 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
97-103
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:10432305-Amino Acid Sequence, pubmed-meshheading:10432305-Cell Line, pubmed-meshheading:10432305-Cloning, Molecular, pubmed-meshheading:10432305-Conserved Sequence, pubmed-meshheading:10432305-Eukaryotic Initiation Factor-2, pubmed-meshheading:10432305-Gene Products, gag, pubmed-meshheading:10432305-Genes, Dominant, pubmed-meshheading:10432305-HIV Antigens, pubmed-meshheading:10432305-HIV-1, pubmed-meshheading:10432305-HeLa Cells, pubmed-meshheading:10432305-Humans, pubmed-meshheading:10432305-Models, Biological, pubmed-meshheading:10432305-Molecular Sequence Data, pubmed-meshheading:10432305-Molecular Weight, pubmed-meshheading:10432305-Mutation, pubmed-meshheading:10432305-Prokaryotic Initiation Factor-2, pubmed-meshheading:10432305-Protein Binding, pubmed-meshheading:10432305-Protein Biosynthesis, pubmed-meshheading:10432305-RNA, Messenger, pubmed-meshheading:10432305-Recombinant Fusion Proteins, pubmed-meshheading:10432305-Transfection, pubmed-meshheading:10432305-Viral Proteins, pubmed-meshheading:10432305-Yeasts, pubmed-meshheading:10432305-gag Gene Products, Human Immunodeficiency Virus
pubmed:year
1999
pubmed:articleTitle
Cloning and characterization of hIF2, a human homologue of bacterial translation initiation factor 2, and its interaction with HIV-1 matrix.
pubmed:affiliation
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K. stuart.wilson@umist.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't