Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.21.3 (deoxyribonuclease)
 1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The proteins of the secretory granules of the rat parotid gland were characterized by sodium dodecylsulfate gel electrophoresis, by chromatography of [3-H]proline-labeled proteins on DEAE-cellulose and by amino acid analysis. Sodium dodecylsulfate gel electrophoresis of the secretory granule content showed five principal proteins and a limited number of minor components. Only two of the principal bands could be identified as known secretory enzymes of the parotid gland. One was identified as the alpha-amylase and one as deoxyribonuclease. Peroxidase and ribonuclease form minor portions of the secretory proteins. The other three major proteins constitute, together, about 60% by weight, of the secretory granule content proteins. Of these, one which represents more than 30% of the total granule protein was found to contain uniquely high amounts of leucine residues (21 mole%). Another one of these principal proteins was relatively rich in cysteine residues (7 mole%). The fifth principal protein was found to contain high amounts of proline (28 mole%) glutamic acid (17 mole%) and glycine (18 mole%) residues. Its amino acid composition was very similar to that of the proline-se granules. This protein, however, differed from the "membranous" proline-rich proteins by several criteria. Two minor glycoproteins of the secretory granule content were also found to be rich in proline residues (37 mole%). As with the other proline-rich proteins of the granule, they contained no sulphur-containing amino acids, stained faintly pink with Coomassie Blue and were underestimated by the Lowry method. They differ however, from all the other proline-rich proteins of the granule by having a significantly higher content of threonine, less glycine (9 mole%) and much less glutamic acid (3 mole%). Of the principal proteins, only the deoxyribonuclease and the half-cystine-rich proteins were positively stained by periodic acid Schiff staining. The possible functions of the leucine-rich, the half cystine-rich and the various proline-rich proteins are discussed.
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PMID:The proteins of the content of the secretory granules of the rat parotid gland. 112 45

Two cysB mutant alleles of S. typhimurium have been cloned onto pBR vectors. The product of the constitutive cysBc 1352 allele present on the plasmid was found to fulfill regulatory functions: as an activator of the cysteine regulon and as an autorepressor. CysB70 auxotrophic mutation impairs both regulatory functions cysB protein. Transfer of the clones cysBc 1352 allele from E. coli to S. typhimurium and from S. typhimurium to E. coli and biochemical analysis of transformants suggest involvement of a restriction-modification system in the constitutive expression of the cysteine regulon.
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PMID:Cloning of cysB mutant alleles of S. typhimurium. 330 Jan 14

The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.
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PMID:Generation of a hybrid sequence-specific single-stranded deoxyribonuclease. 368 86

Herpes simplex virus type 1 (HSV-1) encodes a deoxyribonuclease that is frequently referred to as alkaline nuclease (AN) because of its elevated pH optimum. Studies with recombinant viruses which contain deletions in the HSV-1 gene encoding AN have indicated that this enzyme is required for efficient virus replication and therefore represents a potential target for novel antiviral therapies. A simple colorimetric assay for deoxyribonuclease activity employing a DNA-methyl green substrate was adapted for use in a high-throughput screen to identify small molecule inhibitors of this enzyme. This screen identified 1,2-benzoisothiazolin-3-one as a specific inhibitor of AN, since it exhibited activity against AN but was completely inactive against bovine pancreatic DNaseI. Subsequent studies revealed that this compound most likely inhibited AN by forming disulfide linkages with one or more exposed cysteine residues on the surface of the enzyme and that AN was sensitive to sulfhydryl-group-modifying reagents in general. These results demonstrated the utility of this DNA-methyl green substrate-based assay in both the rapid identification and the characterization of novel small molecule inhibitors of the AN encoded by HSV-1 and other herpesviruses.
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PMID:A colorimetric assay for high-throughput screening of inhibitors of herpes simplex virus type 1 alkaline nuclease. 1139 38

Single-molecule real-time (SMRT) sequencing can be used to identify a wide variety of chemical modifications of the genome, such as methylation. Here, we applied this approach to identify N6-methyl-adenine (m6A) and N4-methyl-cytosine (m4C) modification in the genome of Bacillus pumilus BA06. A typical methylation recognition motif of the type I restriction-modification system (R-M), 5'-TCm6AN8TTGG-3'/3'-AGTN8m6AACC-5', was identified. We confirmed that this motif was a new type I methylation site using REBASE analysis and that it was recognized by a type I R-M system, Bpu6ORFCP, according to methylation sensitivity assays in vivo and vitro. Furthermore, we found that deletion of the R-M system Bpu6ORFCP induced transcriptional changes in many genes and led to increased gene expression in pathways related to ABC transporters, sulfur metabolism, ribosomes, cysteine and methionine metabolism and starch and sucrose metabolism, suggesting that the R-M system in B. pumilus BA06 has other significant biological functions beyond protecting the B. pumilus BA06 genome from foreign DNA.
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PMID:A novel DNA methylation motif identified in Bacillus pumilus BA06 and possible roles in the regulation of gene expression. 3208 59