Disease relevance of DCLRE1C

• We previously showed that these components, when bound with histones on plasmids containing the region, confer on the complex a pattern of hypersensitivity to nuclease digestion similar to that in the nucleus [1].
• The transcriptionally active ev-3 and inactive ev-1 endogenous retrovirus loci in chick cells differ in that ev-3 is undermethylated, preferentially sensitive to DNase I digestion, and contains nuclease hypersensitive sites in each of its two long terminal repeats [2].
• In this cell type, the ev-3 preintegration site is organized in a nuclease-resistant conformation, while the ev-3 provirus is in a nuclease-sensitive conformation and is transcribed [3].
• On the basis of the nuclease S1 protection assay with uniformly labeled single-stranded pRLC429 DNA, subcloned into M13mp18 phage vector, we conclude that the rat atrial muscle also contains MLC2 of the ventricular type [4].
• Both 4 S RNA and the 10 S RNP are potent inhibitors of translation of a variety of mRNAs such as chick muscle poly(A)+ mRNA, rabbit globin mRNA, EMC virus RNA, and poly(A)- and mRNA of rat liver in micrococcal nuclease-treated rabbit reticulocyte lysate [5].

High impact information on DCLRE1C

• These fragments do not result from bulk nucleosome phasing in vivo, but arise from micrococcal nuclease cleavages internal to the core particle, at roughly 10-base pair intervals and at AT-rich sequences [6].
• We believe that some aspect of DNA sequence is translated into an altered DNA structure in chromatin and that it is this altered structure that is recognized by s1 nuclease and possibly by certain chromosomal proteins [7].
• Using nuclease digestion, one can progressively cleave DNA from the loops, thereby isolating residual DNA that is progressively closer to the nuclear matrix anchorage sites [8].
• Furthermore, a 115 base pair DNA fragment contained within this nuclease-sensitive region can be excised by Msp I digestion and released from nuclei, in at least 50% yield [9].
• A 200 base pair region at the 5' end of the chicken adult beta-globin gene is accessible to nuclease digestion [9].

Chemical compound and disease context of DCLRE1C

• Analysis of nuclease hypersensitivity of regions flanking the estrogen-dependent, chicken apoVLDLII gene has revealed an hepatic, DNaseI hypersensitive site whose sensitivity is influenced by both the developmental stage and sex of the bird [10].

Biological context of DCLRE1C

• Genetic analyses confirm this suggestion as we have demonstrated an epistatic relationship between 53BP1 and the NHEJ genes, Ku70 and Artemis, but not with Rad54, a gene essential for repair of DSBs by homologous recombination [11].
• Furthermore, in contrast to the uninsulated reporter genes, chromatin over the insulated genes retains nuclease accessibility and histone hyperacetylation [12].
• Nuclease protection experiments on intact nuclei show that at early stages of embryonic development, the CACCC site is occupied and the Pal site is vacant, but as development progresses, the Pal site is filled gradually and the CACCC site loses its bound protein [13].
• RNA interference is an evolutionarily conserved gene-silencing pathway in which the nuclease Dicer cleaves double-stranded RNA into small interfering RNAs [14].
• Alternatively, the scaffold DNA was prepared from micrococcal nuclease-digested intact chromosomes using sucrose gradients containing 2M NaCl [15].

Anatomical context of DCLRE1C

• The structure of chicken erythrocyte and chicken liver chromatin has been studied by enzymatic digestion with micrococcal nuclease and DNAase I [16].
• This suggests that active genes are preferentially digested by deoxyribonuclease I. In contrast, treatment of red cell nuclei with staphylococcal nuclease results in no preferential digestion of active globin genes [17].
• Fragments of 20-25, 40-50, 90-110, and 160-180 base pairs (bp), along with intermediate-size pieces were isolated by preparative gel electrophoresis of a limited micrococcal nuclease digest of calf thymus DNA [18].
• Nuclei of chicken oviduct cells and of erythrocytes, and preparations of 'naked' DNA were digested with DNase I and with micrococcal nuclease [19].
• Correct and efficient transient expression directed by the lysozyme promoter was found in both of these cell lines, as determined by S1 nuclease mapping and Northern blot analysis of the RNAs made [20].

Associations of DCLRE1C with chemical compounds

• SV40 DNA replicated in the presence of cycloheximide was more sensitive to staphylococcal nuclease digestion and had a lower superhelical density than viral DNA replicated in the absence of this drug [21].
• In contrast to this, over 75% of the 5-methylcytosine was protected from nuclease digestion by chromatin proteins [22].
• Of particular interest is the presence in 50S hnRNP of a nuclease-resistant region (24-28 nucleotides long) in both IVS immediately upstream from the putative lariat branch site in an RNA splicing intermediate [23].
• A region of about 200 base pairs 5' to the chicken beta A-globin gene, which contains sites sensitive to nuclease S1, to several restriction endonucleases, and to very low levels of DNase I, also contains DNA structures that are preferentially sensitive to bromoacetaldehyde [24].
• This observation argues against the possibility that the generation of nucleosomal DNA following drug treatment of nuclei is due to an activation of endogenous nuclease by bleomycin and strongly suggests that the drug has a unique feature of action on chromatin [25].

Physical interactions of DCLRE1C

• In this paper, electrophoretic mobility shift assays (EMSAs) and S1 nuclease treatment are used to demonstrate that the RBF-maltose binding protei (MBP) fusion protein binds to single-stranded DNA of its element [26].

Enzymatic interactions of DCLRE1C

• Rather, an analysis of the fragmentation of the ovalbumin chromatin as a function of digestion extent suggested a mechanism in which the heightened sensitivity resulted from the collective expansion of the nuclease cutting sites in the linker regions of the ovalbumin chromatin because the gene was in an unfolded conformation [27].

Other interactions of DCLRE1C

• 53BP1 contributes to survival of cells irradiated with X-ray during G1 without Ku70 or Artemis [28].
• Using the techniques of runoff transcription, primer extension, and S1 nuclease protection, we demonstrate that there is a third c-myc exon of approximately equal to 345 base pairs (bp) located 0.7 kbp upstream of the 5' end of the v-myc homology [29].
• We studied the developmental and tissue-specific expression of phospholamban mRNA using nuclease mapping analysis [30].
• We also present evidence for extensive, differentiation-dependent alterations in nuclease accessibility at the lysozyme promoter without alterations of nucleosome and transcription factor occupancy [31].
• We have precisely determined the positions of the first three exons for the major chicken vitellogenin gene (VTG II) by a combination of S1 nuclease protection, primer extension and DNA sequencing experiments [32].

Analytical, diagnostic and therapeutic context of DCLRE1C

• RNA transcribed in vivo from the chicken ovalbumin gene has been analyzed in detail in the 3' region of the gene using nuclease S1 mapping and Northern blotting [33].
• Fractions of homogeneously-sized supranucleosomal particles can be obtained in high yield and purity from various types of cells by brief micrococcal nuclease digestion (10 or 20 s) of condensed chromatin in 100 mM NaCl followed by sucrose gradient centrifugation and agarose gel electrophoresis [34].
• High-affinity nucleoprotein acceptor sites for the avian oviduct progesterone receptor (PR) have been enriched by a combination of nuclease digestion and centrifugation [35].
• Micrococcal nuclease digestion and electron microscopy studies indicated that there is heterogeneity in the spacings at which core particles are assembly on the DNA [36].
• New studies on chromatin fiber morphology, using the technique of scanning force microscopy (SFM), have caused us to reexamine recent analysis of nuclease digestion of chromatin [37].

References