Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

The DNA sequence of a naturally occurring alcohol dehydrogenase null activity allele, AdhnAC14, has eight extra nucleotides (in two groups of four) in the second intron, commencing six bases 3' from the 5' splice site. A stop codon was also found in exon 2. S1 nuclease protection experiments have shown that the insertions in intron 2 disrupt the correct splicing of intron 2. The null allele produces a transcript approximately 100 bases longer than the normal mature adult transcript, and the amount of the null allele transcript is only about 10% of the normal level.
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PMID:Aberrant splicing of a naturally occurring alcohol dehydrogenase null activity allele in Drosophila melanogaster. 212 91

The mouse has three genes (Adh) encoding alcohol dehydrogenase (ADH) enzymes of different tissue specificity and catalytic properties. Identified regulatory loci are known to affect the expression of Adh-1 and Adh-3, which are closely linked on chromosome 3. The Adh-1 gene product is expressed predominantly in liver, and its mRNA product is androgen-inducible in kidney. In this study, genomic clones of Adh-1 were obtained from a Balb/cJ DNA library. The nucleotide sequences of all exons, intron/exon boundaries and 5'- and 3'-flanking regions were obtained. The gene spans nearly 13 kb and is divided into nine exons and eight introns. The transcription start point of this gene was determined by S1 nuclease mapping studies and presumptive regulatory regions in the 5'-flanking regions were identified, including a TATA box and a glucocorticoid-responsive element. A restriction fragment length polymorphism in the Adh-1 gene was identified among inbred strains and mapped at the [Adh-1, Adh-3] complex on chromosome 3. An additional 'Adh-like' sequence in the genome was also mapped to chromosome 3 approx. 9 centiMorgans from Adh-1.
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PMID:Molecular analysis of mouse alcohol dehydrogenase: nucleotide sequence of the Adh-1 gene and genetic mapping of a related nucleotide sequence to chromosome 3. 289 58

Human alcohol dehydrogenase (ADH) exists as a heterogeneous group of isozymes capable of oxidizing a wide variety of aliphatic and aromatic alcohols. The five distinct human ADH subunits, each encoded by a separate gene, are differentially expressed during development and are subject to tissue-specific regulation. To analyze the organization and regulation of human ADH genes we first isolated a cDNA clone (pADH12) encoding the 3' portion of the beta ADH gene. In the current study pADH12 was used to screen a human genomic library, and several overlapping and nonoverlapping clones were selected. Hybridization and partial nucleotide sequence analyses of the clones indicated that three full-length human ADH genes encoding the alpha, beta, and gamma subunits were isolated. Human genomic DNA hybridization results indicate that the alpha, beta, and gamma ADH genes form a closely related gene family and suggest that the other known human ADH genes (i.e. those encoding the pi and chi subunits) share a more distant evolutionary relationship. Nucleotide sequence analysis of the beta ADH gene reveals that the coding region is interrupted by eight introns and spans approximately 15 kilobases. A presumptive transcription initiation site for the beta ADH gene was located by S1 nuclease mapping at a position 70 base pairs upstream of the start codon. The 5' flanking region possesses a TATA box promoter element as well as two tandem DNA sequences which display homology to previously examined glucocorticoid-responsive elements.
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PMID:Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. 293 33

Hybrid genes containing mRNA encoding sequences for herpes virus thymidine kinase (tk), chloramphenicol acetyltransferase (CAT), or Drosophila alcohol dehydrogenase (Adh), ligated to truncated Drosophila melanogaster heat-shock protein 70 (hsp 70) gene promoters or to synthetic sequences containing one or several copies of a previously defined heat-shock consensus sequence, were transfected into cultured Drosophila line S3 cells. Each construction was then assayed for gene expression at 25 degrees C and 37 degrees C, using a CAT enzyme assay, slot blot hybridization, or S1 nuclease protection analysis. In the Drosophila cell transient expression assay system, we found that deletions extending beyond position -97, or synthetic constructions containing a single heat shock consensus sequence, were not induced by high-temperature shock. In constructions containing deletions extending to position -186, -130, or -97, in the hsp 70 promoter, and in synthetic constructions containing tandemly spaced heat-shock consensus sequences mRNA transcription was greatly induced by high temperature.
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PMID:Natural and synthetic heat shock protein gene promoters assayed in Drosophila cells. 309 68

The DNA sequence of the gene for the fermentative yeast alcohol dehydrogenase has been determined. The structural gene contains no introns. The amino acid sequence of the protein as determined from the nucleotide sequence disagrees with the published alcohol dehydrogenase isozyme I (ADH-I) sequence for 5 of the 347 amino acid residues. At least one, and perhaps as many as four, of these differences is probably due to ADH-I protein heterogeneity in different yeast strains and not to sequencing errors. S1 nuclease was used to map the 5' and 3' ends of the ADH-I mRNA. There are two discrete, mature 5' ends of the mRNA, mapping 27 and 37 nucleotides upstream of the translation initiating ATG. These two equally prevalent termini are 101 and 91 nucleotides, respectively, downstream from a TATAAA sequence. Analysis of the 3' end of ADH-I mRNA disclosed two minor ends upstream of the major poly(A) addition site. These three ends map 24, 67, and 83 nucleotides, respectively, downstream from the translation-terminating TAA triplet. The sequence AA-TAAG is found 28 to 34 nucleotides upstream of each ADH-I mRNA poly(A) addition site. Sequence comparisons of these three 3' ends with those for four other yeast mRNAs yielded a 13-nucleotide consensus sequence to which TAAATAAGA is central. All of the known yeast poly(A) addition sites map at or near the A residue of a CTA site 25 to 40 nucleotides downstream from this consensus octamer.
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PMID:The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. 627 22

The complete nucleotide sequence of the glucose-repressed alcohol dehydrogenase II gene (ADR2) from yeast has been established together with its 5'- and 3'-flanking regions. The limits of the gene have been determined by reverse transcriptase sequencing of the 5'-ends and by S1 nuclease mapping of the 3'-ends of the mature ADR2 mRNA. Comparison of the alcohol dehydrogenase I gene (ADC1) sequence (Bennetzen, J. L., and Hall, B.D. (1982) J. Biol. Chem. 257, 3018-3025) with that of ADR2 indicated four regions of sequence conservation in the 5'-flanking DNAs. One of these conserved regions contains the sequence TCAAG which may function as a yeast cap sequence. The coding sequence of ADR2 is 89% homologous with that of ADC1 and exhibits a bias in its codon utilization. Evidence is presented that the intergenic region at the 3'-end of the ADR2 gene is less than 550 base pairs.
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PMID:Nucleotide sequence of the yeast alcohol dehydrogenase II gene. 633 60

A novel method has been developed for determining the location of RNA termini and intron-exon boundaries using genomic clones. RNA is hybridized to a single-stranded M13 phage derivative of the genomic fragment of interest. S1 nuclease digestion results in an RNA-DNA hybrid corresponding to any transcript protected by the insert. Hydrolysis of the RNA with alkali, hybridization of the DNA with the opposite-strand M13 derivative of the genomic fragment and S1 nuclease digestion yields a mixture of pure exons. This mixture is analyzed by agarose gel electrophoresis and is cloned using excess blunt-ended M13 phage vector. Plaques that contain inserts are identified by transfer to nitrocellulose and hybridization to the genomic insert and are used without further purification. Cloning junctions are then determined by partial sequence analysis. These very nearly correspond to intron-exon boundaries or to either end of the transcript. When applied to the alcohol dehydrogenase gene from Drosophila, this method revealed clear differences between the 5' ends of embryo and adult transcripts both by blot hybridization and by analysis of 23 independent exon clones. In embryos, the mature transcript is apparently derived from three exons and in adults from four with the difference lying in the 5' untranslated portion of the transcript. The method should be particularly valuable for mapping and cloning transcripts that are rare or are not polyadenylated.
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PMID:Cloning exons of mapping of transcription: characterization of the Drosophila melanogaster alcohol dehydrogenase gene. 641 Mar 56

We have obtained correct transcription of the cloned alcohol dehydrogenase (Adh) gene of Drosophila melanogaster after DNA-mediated gene transfer into Drosophila cells in culture. Supercoiled plasmids, each containing various regions of the Adh gene cloned in pBR327, were introduced into Schneider line 2 (SL2) cells by the calcium phosphate-DNA transfection technique. Although these cells do not normally express their endogenous Adh genes, they do express the exogenous genes as shown by primer extension and nuclease S1 analyses of RNA isolated 48 hr after transfection. The resulting alcohol dehydrogenase (ADH) transcripts, both the larval and adult types, have the correct 5' ends and are properly spliced. The transfected cells have also acquired ADH enzyme activity. The levels of enzyme activity and of ADH protein crossreacting material in cells transfected with different Adh plasmids correlate directly with the level of ADH transcripts. When a mutant Adh gene cloned from an ADH-negative mutant fly with a defect in the splicing of ADH RNA is transfected into the Schneider line 2 cells, the resulting ADH RNA is not spliced properly and there is no synthesis of ADH; thus, the mutant gene transfection into cell culture mimics the mutant phenotypes observed in the mutant fly.
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PMID:Cloned Drosophila alcohol dehydrogenase genes are correctly expressed after transfection into Drosophila cells in culture. 642 22

The alcohol dehydrogenase (ADH; alcohol: NAD+ oxidoreductase, EC 1.1.1.1) gene (Adh) of Drosophila melanogaster was isolated by utilizing a mutant strain in which the Adh locus is deleted. Adult RNA from wild-type flies was enriched in ADH sequences by gel electrophoresis and then used to prepare labeled cDNA for screening a bacteriophage lambda library of genomic Drosophila DNA. Of the clones that hybridized in the initial screen, one clone was identified that hybridized with labeled cDNA prepared from a wild-type Drosophila strain but did not hybridize with cDNA prepared from an Adh deletion strain. This clone was shown to contain ADH structural gene sequences by three criteria: in situ hybridization, in vitro translation of mRNA selected by hybridization to the cloned DNA, and comparison of the ADH protein sequence with a nucleotide sequence derived from the cloned DNA. Comparison of the restriction site maps from clones of three different wild-type Drosophila strains revealed the presence of a 200-nucleotide sequence in one strain that was absent from the other two strains. The ADH mRNA sequences were located within the cloned DNA by hybridization mapping experiments. Two intervening sequences were identified within Adh by S1 nuclease mapping experiments.
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PMID:Isolation and partial characterization of the Drosophila alcohol dehydrogenase gene. 677 76

Twenty-three propane- and butane-utilizing bacteria were isolated from soil samples collected from oilfields. Three of them have been identified as Rhodococcus sp. IMT35, Pseudomonas sp. IMT37 and Pseudomonas sp. MT40. SDS-PAGE analysis of the membrane of Rhodococcus sp. IMT35 revealed the presence of at least four polypeptides induced by propane. Polyclonal antibody raised against a 58 kDa polypeptide from Rhodococcus sp. IMT35 specifically detected bacteria which were actively utilizing propane or butane. Immunoscreening of a genomic library in lambdagt11 with this antibody resulted in isolation of a clone containing a 4.9 kb EcoRI genomic DNA fragment. This 4.9 kb DNA fragment was found to hybridize specifically with organisms which could grow on propane or butane. This fragment could therefore be used as a probe for detection of such bacteria. A 2.3 kb fragment having an ORF encoding a polypeptide of 54 kDa was identified by screening a genomic library of Pseudomonas sp. IMT37 with this 4.9 kb EcoRI fragment. The sequence of the ORF (designated orf54) was found to be novel. Primer extension and S1 nuclease mapping showed that transcription of the ORF starts at base 283 and it had sequences upstream similar to that of a Pseudomonas promoter (-12, -24 type). Disruption of the ORF by a kanamycin ('kan') cassette prevented the organism from growing on any alkane but did not affect its ability to utilize the respective alkanols and acids, indicating that alcohol dehydrogenase and subsequent steps in the pathway remained unaltered. The mutants had no detectable level of butane monooxygenase activity. Therefore, the product of this gene plays a crucial role in the first step of the pathway and is an essential component of monooxygenase. The findings imply that this bacterium either employs a common genetic and metabolic route or at least shares the product of this gene for utilization of many alkanes.
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PMID:A novel gene encoding a 54 kDa polypeptide is essential for butane utilization by Pseudomonas sp. IMT37. 1153 88


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