rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1-3
|
pubmed:dateCreated |
1990-11-13
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pubmed:abstractText |
Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0006-3002
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
1050
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
160-2
|
pubmed:dateRevised |
2009-7-24
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pubmed:meshHeading |
pubmed-meshheading:2119810-HeLa Cells,
pubmed-meshheading:2119810-Humans,
pubmed-meshheading:2119810-Kinetics,
pubmed-meshheading:2119810-Lysine,
pubmed-meshheading:2119810-Peptide Initiation Factors,
pubmed-meshheading:2119810-Protein Biosynthesis,
pubmed-meshheading:2119810-Protein Processing, Post-Translational,
pubmed-meshheading:2119810-Puromycin,
pubmed-meshheading:2119810-RNA, Transfer, Met,
pubmed-meshheading:2119810-RNA-Binding Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
The role of mammalian initiation factor eIF-4D and its hypusine modification in translation.
|
pubmed:affiliation |
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|