Linked Life Data

8307948

Source:http://linkedlifedata.com/resource/pubmed/id/8307948

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-3-17
pubmed:abstractText
Eukaryotic translation initiation factor eIF-5A (formerly eIF-4D) is thought to function in protein synthesis by promoting synthesis of the first peptide bond because it stimulates methionyl-puromycin formation in vitro. eIF-5A is encoded by two genes (TIF51A and TIF51B) in Saccharomyces cerevisiae; the protein and its hypusine modification are essential for cell viability. To analyze the factor's function in vivo, we expressed from the repressible GAL promoter a functional but unstable eIF-5A fusion protein (R-eIF-5A) with an NH2-terminal arginine which is subject to rapid turnover through the NH2-terminal end rule proteolytic pathway. When the conditional mutant strain is shifted from galactose to glucose medium, the rapid disappearance of R-eIF-5A protein occurs within one generation, causing an immediate inhibition of cell growth. However, eIF-5A-depleted cells synthesize protein at about 70% of the wild type rate and exhibit only a slight change in polysome profiles reflecting a subtle defect in a late step of translation initiation. These results suggest that the activity of eIF-5A may not be absolutely essential for general protein synthesis. Rather, eIF-5A may be selectively required for translation of certain mRNAs and/or may be involved in some other aspect of cell metabolism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3934-40
pubmed:dateRevised
2009-7-24
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae.
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.