Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.1 (S1 nuclease)
 3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three isoforms of the glycolytic enzyme enolase are present in mammals and birds. During development, a switch from the alpha to the beta form takes place in skeletal muscle. In order to investigate the molecular basis of this developmental transition of enolase isoforms, we extracted total RNA from limbs of mouse embryos of different ages, and from cultures of embryonic and fetal myogenic cells. The beta message was detected in limbs from 16-day-old fetuses by Northern-blot analysis and its level was found to increase in newborn and adult muscle; no significant amount of beta mRNA was present in samples from earlier developmental stages, which did however express high levels of the muscle-specific actin mRNA. Analysis of RNA extracted from embryonic and fetal myoblasts differentiated in culture revealed that the level of beta mRNA is about 9-fold higher in fetal myotubes than in embryonic myotubes, although the level of muscle actin is comparable in both types of myotubes. These results were confirmed by S1 nuclease protection experiments. Our data show that the appearance of beta enolase transcripts temporally correlates with the formation of the second generation of muscle fibers and suggest that the developmental transition from alpha to beta enolase is linked to a developmental program which takes place in fetal but not in embryonic muscle.
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PMID:Differential expression of muscle-specific enolase in embryonic and fetal myogenic cells during mouse development. 209 May 19

In mammals there are at least three isoforms of the glycolytic enzyme enolase encoded by three similar genes: alpha, beta and gamma. In this report we describe the isolation and characterization of the human alpha-enolase locus. The gene appears to exist as a single copy in the haploid genome and is composed of 12 exons distributed over more than 18,000 bases. The structure of this gene has a high degree of similarity to that of the human and rat gamma-enolase genes, with identical positions for all the intron regions. Primer extension and S1 nuclease protection experiments indicate that transcription is initiated at multiple sites. The putative promoter region, like that of other house-keeping genes, lacks canonical TATA and CAAT boxes, is extremely G + C-rich and contains several potential SP1 binding sites. Furthermore, various sequences similar to known regulatory elements were detected.
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PMID:Structure of the human gene for alpha-enolase. 237 81

Neuron-specific (gamma gamma) enolase (NSE) is an isoenzyme form of glycolytic enzyme, enolase. We isolated genomic clones for NSE and clarified NSE gene structures. The NSE-gene spanned about 9 kb and consisted of twelve exons and eleven introns. Multiple transcriptional start points were identified by a combination of S1 nuclease mapping and primer extension analysis. In the 5'-flanking region we found a TATA-like sequence TCTATAGGC which was only partially homologous to the consensus sequence, but we did not find a CAAT box. The sequence in the immediate 5'-flanking region was of a relatively high G + C content and contained GC-box-like clusters that did not correspond to the typical GC box. In addition, we found seven classes of the repeated sequences. In the introns 1, 5 and 10 there were tandem repeats (GT)33, (GT)21 and (GT)24, respectively. The 3' end contains a single polyadenylation site and an identifier sequence 2 kb downstream from the poly(A)-addition site. The in vitro cell-free transcription of the truncated genomic DNA fragment using HeLa cell extract showed that the transcription start points have been correctly identified and the putative promoter sequences appear to be functional.
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PMID:The structure and expression of neuron-specific enolase gene. 245 52

We report here the isolation and characterization of the human gene for the beta or muscle-specific isoform of the glycolytic enzyme enolase. The nucleotide sequence analysis revealed structural features, such as organization as 11 coding exons, the first exon consisting of an untranslated sequence and hence resembling sequences of the other two members of the gene family, the alpha and gamma enolase genes. The beta enolase locus spans about 6 kbp genomic DNA. Sequences matching the consensus sequence for muscle-specific regulatory factors are present in the 5'-flanking region and within the first intron. A combination of primer extension, S1 nuclease protection and RNA-sequencing experiments indicates that the gene has a unique transcriptional start site, 26 bp downstream of a TATA-like box; the differential usage of two donor sites within the untranslated exon I generates two alternatively spliced transcripts. The existence of the two mRNA, differing from one another in the presence or absence of a 42-nucleotide fragment in the leader sequence, was confirmed by cloning the corresponding cDNA using the rapid amplification of cDNA ends strategy. Secondary-structure predictions indicated that the leader sequences of the spliced forms could form hairpin structures with different free energies of formation, suggesting translational control.
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PMID:Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA. 851 87

Rapid modulation of RNA function by endoribonucleases during physiological responses to environmental changes is known to be an effective bacterial biochemical adaptation. We report a molecular mechanism underlying the regulation of enolase (eno) expression by two endoribonucleases, RNase G and RNase III, the expression levels of which are modulated by oxygen availability in Escherichia coli. Analyses of transcriptional eno-cat fusion constructs strongly suggested the existence of cis-acting elements in the eno 5' untranslated region that respond to RNase III and RNase G cellular concentrations. Primer extension and S1 nuclease mapping analyses of eno mRNA in vivo identified three eno mRNA transcripts that are generated in a manner dependent on RNase III expression, one of which was found to accumulate in rng-deleted cells. Moreover, our data suggested that RNase III-mediated cleavage of primary eno mRNA transcripts enhanced Eno protein production, a process that involved putative cis-antisense RNA. We found that decreased RNase G protein abundance coincided with enhanced RNase III expression in E. coli grown anaerobically, leading to enhanced eno expression. Thereby, this posttranscriptional up-regulation of eno expression helps E. coli cells adjust their physiological reactions to oxygen-deficient metabolic modes. Our results revealed a molecular network of coordinated endoribonuclease activity that post-transcriptionally modulates the expression of Eno, a key enzyme in glycolysis.
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PMID:The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli. 3175 58