pubmed-article:8307948 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C0030943 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C0115621 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C1414360 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
pubmed-article:8307948 | lifeskim:mentions | umls-concept:C0333668 | lld:lifeskim |
pubmed-article:8307948 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:8307948 | pubmed:dateCreated | 1994-3-17 | lld:pubmed |
pubmed-article:8307948 | 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. | lld:pubmed |
pubmed-article:8307948 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8307948 | pubmed:language | eng | lld:pubmed |
pubmed-article:8307948 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8307948 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8307948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8307948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8307948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8307948 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8307948 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8307948 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8307948 | pubmed:author | pubmed-author:HersheyJ WJW | lld:pubmed |
pubmed-article:8307948 | pubmed:author | pubmed-author:KangH AHA | lld:pubmed |
pubmed-article:8307948 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8307948 | pubmed:day | 11 | lld:pubmed |
pubmed-article:8307948 | pubmed:volume | 269 | lld:pubmed |
pubmed-article:8307948 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8307948 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8307948 | pubmed:pagination | 3934-40 | lld:pubmed |
pubmed-article:8307948 | pubmed:dateRevised | 2009-7-24 | lld:pubmed |
pubmed-article:8307948 | pubmed:meshHeading | pubmed-meshheading:8307948-... | lld:pubmed |
pubmed-article:8307948 | pubmed:meshHeading | pubmed-meshheading:8307948-... | lld:pubmed |
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pubmed-article:8307948 | pubmed:meshHeading | pubmed-meshheading:8307948-... | lld:pubmed |
pubmed-article:8307948 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8307948 | pubmed:articleTitle | Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. | lld:pubmed |
pubmed-article:8307948 | pubmed:affiliation | Department of Biological Chemistry, School of Medicine, University of California, Davis 95616. | lld:pubmed |
pubmed-article:8307948 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8307948 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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