PubMed · 181628
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G M Boriskina, Iu V Postnov. 1976. [Natriuretic factor].. https://pubmed.ncbi.nlm.nih.gov/181628/
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UAP56 (U2AF65 associated protein) is a member of the DEAD-box helicase family. Helicases are essential enzymes generally involved in the metabolism of nucleic acids. The gene encoding a member of DEAD-box family was cloned and characterized from the human malaria parasite Plasmodium falciparum. PfU52 is homologous to UAP56 and contains the RNA-dependent ATPase, RNA helicase and RNA binding activities. Using the parasite extract we report that PfU52 is involved in splicing reaction. Site-directed mutagenesis studies indicate that the conserved residues glycine 181, isoleucine 182 and arginine 206 are involved in RNA binding and this activity is required for the enzymatic activities of PfU52. PfU52 is expressed in all the intraerythrocytic developmental stages of the parasite. In the present study we have reported the detailed characterization of PfU52 from P. falciparum and these results advance the knowledge regarding the function of UAP56 in general.
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The Snf-Swi complex of the yeast Saccharomyces cerevisiae has been shown to control gene expression by controlling chromatin structure. We have analyzed the promoter of the SUC2 gene, a gene strongly controlled by Snf-Swi, by a high resolution analysis of micrococcal nuclease digests. This analysis suggests that there are at least four nucleosomes positioned over the SUC2 TATA and UAS regions under conditions repressing SUC2 transcription. Under derepressing conditions this entire promoter region is much more sensitive to MNase digestion. Analysis of an snf2 Delta mutant demonstrates that even under derepressing conditions the SUC2 promoter is resistant to MNase digestion. Thus, the Snf-Swi complex appears to control chromatin structure over both the SUC2 TATA and UAS regions. The presence of nucleosomes over both promoter regions may explain the strong requirement of SUC2 for Snf-Swi function.