Disease relevance of DED1

• Here, we show that Ded1p purified from Escherichia coli has an ATPase activity, which is stimulated by various RNA substrates [1].
• This and the fact that Ded1p is also required for translating brome mosaic virus RNA2 in yeast thus raise the intriguing possibility that Ded1p is one of the key host factors favored by several evolutionarily related RNA viruses, including the human hepatitis C virus [2].

High impact information on DED1

• Activation by the ded1 element thus may involve effects on the chromatin template that facilitate entry of the transcription machinery, whereas activation by the gal element may involve specific contacts between GAL4 and the transcriptional machinery [3].
• The predicted amino-acid sequence of the SPP81 protein shows extensive similarity to a recently identified family of proteins thought to possess ATP-dependent RNA helicase activity [4].
• The DED1 gene, which encodes a putative RNA helicase, has been implicated in nuclear pre-messenger RNA splicing in the yeast Saccharomyces cerevisiae [5].
• The HIS3-PET56 and DED1 promoter regions associate poorly with histones in vitro, indicating that intrinsic nucleosome stability is a major determinant of preferential accessibility [6].
• In contrast to NER, photolyase rapidly repairs CPDs in non-nucleosomal regions, including promoters of active genes (URA3, HIS3, DED1) and in linker DNA between nucleosomes [7].

Biological context of DED1

• DNA fragments from the nuclease sensitive promoter region of DED1 were used for nucleosome reconstitution in vitro [8].
• Two additional ORFs, with a high homology to S. cerevisiae PET56 and DED1 genes, were mapped upstream and downstream from TdHIS3 and TdMRP51, respectively [9].
• Interestingly, the C-terminal deletion was also suppressed by a high gene dosage of the DED1 gene encoding a putative helicase [10].
• I investigated double-strand-break repair in Saccharomyces cerevisiae cells by measuring the frequencies and types of integration events at the PET56-HIS3-DED1 chromosomal region associated with the introduction of linearized plasmid DNAs containing homologous sequences [11].
• Two tandem ABFI binding sites were found between the HIS3 and DED1 genes, several kilobase pairs from any ARS, indicating that ABFI-binding sites are not restricted to ARSs [12].

Anatomical context of DED1

• The analyses of its suppressor activity, of polysome profiles of ded1 mutant strains, and of synthetic lethal interactions with different translation mutants indicate that the Ded1 protein has a role in translation initiation in S. cerevisiae [13].
• We discuss here our present knowledge of the function of eIF4A and Ded1p, two DEAD-box proteins required for translation in eukaryotic cells [14].
• DEAD-box proteins are involved in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation [15].

Associations of DED1 with chemical compounds

• A thymidine-rich sequence upstream of the DED1 gene of Saccharomyces cerevisiae activated transcription of the CYC1 promoter by RNA polymerase II in vitro [16].

Regulatory relationships of DED1

• The mutagenized TOP2 gene we have used is under the control of the yeast DED1 promoter; this overexpression of TOP2 is designed to avoid isolating mutants that are drug resistant solely because the mutated topoisomerase II has low enzymatic activity [17].

Other interactions of DED1

• The double mutant, srm1-1 ded1-21, could grow at 35 degrees C, but not at 37 degrees C. A revertant of srm1-1 ded1-21 that became able to grow at 37 degrees C acquired another mutation in the SRM1 gene, indicating the tight relationship between SRM1 and DED1 [18].
• Similar effects are observed for mutations in the DED1 gene, which we have isolated as a multicopy suppressor of a temperature-sensitive eIF4E mutation [13].
• Genetic interaction of DED1 encoding a putative ATP-dependent RNA helicase with SRM1 encoding a mammalian RCC1 homolog in Saccharomyces cerevisiae [18].
• DNA unwinding in the CYC1 and DED1 yeast promoters [19].
• In contrast to the SPP81/DED1 gene the DBP1 gene was not essential for cell viability [20].

Analytical, diagnostic and therapeutic context of DED1

• Here, we describe a novel atomic force microscopy (AFM)-based procedure to examine the roles of two yeast helicases, eIF4A and Ded1, previously implicated in translation initiation by genetic and biochemical studies [21].

References