| pubmed-article:3275866 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0035552 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C2700592 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C1979886 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C1265875 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0456962 | lld:lifeskim |
| pubmed-article:3275866 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:3275866 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3275866 | pubmed:dateCreated | 1988-2-10 | lld:pubmed |
| pubmed-article:3275866 | pubmed:abstractText | The suggestion that compensation for overabundant mRNA of the genes for Saccharomyces cerevisiae ribosomal protein (r-protein) L3, L29, or rp59 occurs by translation repression has been reinvestigated. First, analysis of the distribution of these three mRNAs in polysome profiles revealed no differences between normal and mRNA-overproducing strains, indicating that initiation of r-protein translation is not repressed under conditions of mRNA overaccumulation. Second, experiments involving radioactive pulse-labeling of proteins were done by using a modified method of data collection and analysis that allows quantitation and correction for fast decay during the pulse. These measurements revealed that the synthesis rate of the three r-proteins is increased when their mRNA levels are elevated and that their decay rate is also high, with half-lives ranging from a fraction of a minute to more than 10 min. We conclude that accumulation of excess r-protein mRNA has no effect on translation rate; rapid decay of protein during the course of the labeling period can account for the apparent discrepancy between mRNA levels and protein synthesis rates. Yeast r-proteins, when produced in excess, are among the most rapidly degraded proteins so far described. | lld:pubmed |
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| pubmed-article:3275866 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3275866 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3275866 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3275866 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3275866 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3275866 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:3275866 | pubmed:author | pubmed-author:PlutheroF GFG | lld:pubmed |
| pubmed-article:3275866 | pubmed:author | pubmed-author:FriesenJ DJD | lld:pubmed |
| pubmed-article:3275866 | pubmed:author | pubmed-author:MaicasEE | lld:pubmed |
| pubmed-article:3275866 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3275866 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:3275866 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3275866 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3275866 | pubmed:pagination | 169-75 | lld:pubmed |
| pubmed-article:3275866 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3275866 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3275866 | pubmed:articleTitle | The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay. | lld:pubmed |
| pubmed-article:3275866 | pubmed:affiliation | Department of Medical Genetics, University of Toronto, Ontario, Canada. | lld:pubmed |
| pubmed-article:3275866 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3275866 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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