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At least 775 records · Page 43Linked to original sources
PubMed1986

Regulation of protein synthesis in heat-shocked Drosophila cells. Soluble factors control translation in vitro.

We have developed an in vitro translation system from heat-shocked and normal Drosophila cultured cells. The lysates retain regulation of translation typical of the whole cells from which they were prepared, both when programmed by endogenous mRNA and when RNA-dependent. These systems have been used to investigate the mechanism of shutdown of normal protein synthesis and selection of heat shock mRNAs for translation in heat shock in Drosophila. Supplementation of intact RNA-dependent lysates with separated ribosome or supernatant fractions from normal or heat-shocked translation systems showed the normal supernatant fraction could "rescue" normal protein synthesis in a heat shock lysate. Normal ribosomes had no rescuing activity and neither heat shock fraction affected translation in normal lysates. Reconstitution of the system from separated ribosomes and supernatant in normal and mixed combinations showed heat shock and normal ribosomes were both competent to support normal protein synthesis with normal supernatant. Heat shock supernatant did not support normal protein synthesis with ribosomes from either source. We conclude that the factors regulating translation in heat-shocked Drosophila cells are soluble factors in the lysate and that the soluble factors present in the normal lysate are dominant.

Animals↗
PubMed1988

Shifts in configuration of the 5'-noncoding region of a mouse messenger RNA under translational control.

Several major mRNA species of mouse and other mammalian cells occur both as small untranslated ribonucleoprotein particles and as functional molecules associated with ribosomes in polysomes. One of these, that codes for a 21-kDa polypeptide, was analyzed with respect to distribution of sites accessible to RNase T1 in the 5'-noncoding region. This region, which is about 100 nucleotides long, contains several sites that are highly sensitive to the enzyme, as well as many G residues not susceptible to cleavage. The distribution of highly sensitive sites was compared in the active and inactive states of the P21 mRNA present in cytoplasmic extracts by subjecting the extract to limited nuclease digestion followed by separation of partially fragmented polysomes from free messenger ribonucleoprotein particles. The mRNA in polysomes contained two highly sensitive sites, one near the 5' terminus and the other in the middle of the region, next to a sequence potentially capable of Shine-Dalgarno interaction. The untranslated molecules lacked the 5'-proximal site but had several highly accessible sites not present in the active molecules. The initiation AUG showed little accessibility both in polysomes and in messenger ribonucleoproteins. Both forms were quite different from the deproteinized mRNA with respect to distribution of nuclease-sensitive sites. Our results indicate that interaction of the mRNA with cytoplasmic factors strongly affects its conformation in the 5'-noncoding region and that a particular conformation may be important for effective interaction with ribosomal particles during polypeptide chain initiation.

Animals↗
PubMed1980

Transcriptional and translational control of nafenopin-induced ornithine decarboxylase activity in rat liver.

The induction of liver ornithine decarboxylase activity by nafenopin was studied in rats. The alpha-adrenergic antagonist, phentolamine, injected 0.5 hr before nafenopin, greatly potentiated the response. Actinomycin D, injected before nafenopin, did not affect nafenopin-induced ornithine decarboxylase activity whereas the potentiating effect of phentolamine was inhibited. In contrast, administration of actinomycin D 5.0 hr after nafenopin markedly enhanced nafenopin-induced activity. The induction of ornithine decarboxylase activity by nafenopin, as well as the potentiating effect of phentolamine was inhibited by 1,3-diaminopropane and cycloheximide, implying a requirement for synthesis of new enzyme protein for both effects. These results suggest that nafenopin induced ODC through a posttranscriptional mechanism whereas the potentiating effect of phentolamine requires transcription of new messenger RNA.

Animals↗
PubMed2004

Translational profiling: the genome-wide measure of the nascent proteome.

Translation in eukaryotic cells is both physically and temporally separated from transcription. This provides cells with extended options to alter their proteome: (1) directly, by synchronizing translation with an altering transcriptional profile; (2) by imposing a changed translational control over transcripts already present in the transcriptome; or (3) by a combination of (1) and (2). In this paper, recent findings in the controlled translation of the transcriptome using microarray analyses are reviewed. A guide to the current technologies and data analysis is also provided, and future directions in the study of translational control as the interface between the transcriptome and the proteome are outlined. This survey is focused on the yeast Saccharomyces cerevisiae, but the topics covered have universal relevance to the control of translation in eukaryotic cells.

Gene Expression Profiling↗