Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1990-11-13
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.
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
pubmed:meshHeading
pubmed:year
1990
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.