Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.31.1 (micrococcal nuclease)
 2,818 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chromatin structure of two tandemly linked acid phosphatase genes (PHO5 and PHO3) from Saccharomyces cerevisiae was analyzed under conditions at which the strongly regulated PHO5 gene is repressed. Digestion experiments with DNase I, DNase II, micrococcal nuclease and restriction nucleases reveal the presence of five hypersensitive sites at the PHO5/PHO3 locus, two of them upstream of PHO5 at distances of 920 and 370 bp, one in between the two genes and two downstream of PHO3. Specifically positioned nucleosomes are located next to these hypersensitive sites as shown by indirect end-labeling experiments. The positions deduced from these experiments could be verified by monitoring the accessibility of various restriction sites to the respective nucleases. Sites within putative linker regions were about 50-60% susceptible, whereas sites located within nucleosome cores were resistant. Hybridizing micrococcal nuclease digests to a probe from in between the two upstream hypersensitive sites leads to an interruption of an otherwise regular nucleosomal DNA pattern. This shows directly that these hypersensitive sites represent gaps within ordered nucleosomal arrays.
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PMID:Nuclease hypersensitive regions with adjacent positioned nucleosomes mark the gene boundaries of the PHO5/PHO3 locus in yeast. 302 55

We have analyzed the chromatin structure of a phosphate-repressible acid phosphatase gene (PHO5) within yeast nuclei. Under derepressed conditions (low Pi media), the gene is much more sensitive to either DNAse I or micrococcal nuclease digestion than is the repressed gene. We have mapped DNase I hypersensitive sites unique to the active gene near the 5'-end of the acid phosphatase mRNA and within a region presumed to function in the regulation of the gene by Pi. Although the gene is packaged into regularly spaced nucleosomes, no detectable phase relationship exists between nucleosomes and DNA sequence under derepressed conditions, whereas in the repressed state the nucleosomes occur in one predominant phase. These results demonstrate reversible changes in the chromatin structure of a eukaryotic gene system that directly correlate with the functional state of the gene.
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PMID:Modulation of chromatin structure associated with derepression of the acid phosphatase gene of Saccharomyces cerevisiae. 630 84

The reaction of polyuridylic acid with sodium bisulfite produces modified polymers in which up to 95% of the uracil residues have been converted to uracil-6-sulfonate residues. A 91.6% bisulfite-saturated polymer was found to resist hydrolysis by spleen phosphodiesterase and phosphorolysis by polynucleotide phosphorylase. Digestion by pancreatic ribonuclease was successful and gave the bisulfite adduct of uridine-3'-phosphate. Treatment of this nucleotide adduct with acid phosphatase afforded the bisulfite adduct of uridine. The ability of polyuridylic acid to bind to ribosomes, and to stimulate the binding of phenylalanine tRNA to ribosomes was abolished by progressive bisulfite saturation of the polymer. The rate of decline of these functionsf with increasing bisulfite content, was less sharp than the loss of phenyl-alanine coding ability o, the modified polymer.
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PMID:Modification of polyuridylic acid by bisulfite. II: Studies on ribosomal binding and enzymatic hydrolysis. 2419 77