We have investigated the ability of transcripts of the Drosophila melanogaster alcohol dehydrogenase gene to be spliced in Saccharomyces cerevisiae. The alcohol dehydrogenase gene was cloned in S. cerevisiae on a 2 micron DNA-based vector and a hybrid yeast actin-Drosophila alcohol dehydrogenase gene was constructed to demonstrate that transcripts encoded on a 2 micron plasmid could be accurately and efficiently spliced. Transcription of the Drosophila gene occurred in yeast with and without a yeast promoter. The transcripts were polyadenylated and terminated approximately 600 nucleotides distal to the polyadenylation site used in Drosophila. In yeast no splicing of the two introns within the alcohol dehydrogenase coding sequence was detected. However, the leader sequence was apparently spliced using the same 3' splice site as is used in adult flies, but a different 5' splice site. This result may be partly explained by the existence in the Drosophila gene of a sequence which is believed to be required for splicing in S. cerevisiae.
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http://dx.doi.org/10.1002/j.1460-2075.1983.tb01704.x | DOI Listing |
Appl Microbiol Biotechnol
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Department of Life Science and Technology: Tokyo Kogyo Daigaku Seimei Rikogakuin Seimei Rikogakukei, Institute of Science Tokyo, 4259 Nagatsuta-Cho Midzeori-Ku, Yokohama, 226-8501, Japan.
Chiral diaryl alcohols, such as (4-chlorophenyl)(pyridin-2-yl)methanol, are important intermediates for pharmaceutical synthesis. However, using alcohol dehydrogenases (ADHs) in the asymmetric reduction of diaryl ketones to produce the corresponding alcohols is challenging due to steric hindrance in the substrate binding pockets of the enzymes. In this study, the steric hindrance of the ADH from Geotrichum candidum NBRC 4597 (G.
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Department of Biological Hematology, Tours University Hospital, 37000 Tours, France.
Aldehyde dehydrogenases (ALDHs) constitute a group of enzymes that catalyze the oxidation of aldehydes to carboxylic acids. The human ALDH superfamily, including 19 different isoenzymes (ALDH1A1, ALDH1A2, ALDH1A3, AHDH1B1, ALDH1L1, ALDH1L2, ALDH2, ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2, ALDH4A1, ALDH5A1, ALDH6A1, ALDH7A1, ALDH8A1, ALDH9A1, ALDHA16A1, ALDH18A1), displays different key physiological and toxicological functions, with specific tissue expression and substrate specificity. Several studies have established that ALDH are interesting markers for the identification and quantification of human hematopoietic stem cells and cancer stem cells, notably leukemic stem cells.
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College of Food Science and Technology Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution Zhanjiang China.
The study aimed to explore the protective impact of polysaccharide derived from (Turner) C. Agardh (SHP) against ethanol-induced injury in LO2 hepatocytes, along with its potential mechanism of action. A model of alcoholic injury in LO2 cells was established to assess the shielding effect of SHP against liver injury induced by alcohol.
View Article and Find Full Text PDFSemin Liver Dis
December 2024
Inflammation and Immune Mediated Diseases Laboratory of Anhui Province, School of Pharmacy, Anhui Medical University, Hefei, Anhui, P.R. China.
Alcohol-associated liver disease (ALD), primarily caused by chronic excessive alcohol consumption, is a leading cause of chronic liver disease worldwide. ALD includes alcohol-associated steatotic liver, alcohol-associated hepatitis (AH), fibrosis, cirrhosis, and can even progress to hepatocellular carcinoma (HCC). Existing research indicates that the risk factors of ALD are quite numerous.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
Ruhr University Bochum, Analytische Chemie, Universitätsstr 150, 44780, Bochum, GERMANY.
We propose a hybrid electrocatalytic-bioelectrocatalytic reaction cascade integrated on a gas diffusion electrode for CO2 reduction under selective formation of methanol. Ag-Bi2O3 selectively reduces gaseous CO2 to formate at neutral pH conditions. A subsequent enzymatic cascade comprising formaldehyde dehydro-genase and alcohol dehydrogenase, which are both nicotinamide adenine dinucleotide (NAD)-dependent, further reduce formate sequentially to formaldehyde and methanol.
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