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

Genomic clones for 2287 nucleotides of the 5' flanking region, 135 nucleotides of the first exon, and 283 nucleotides of the first intron of the hepatic lipase gene were characterized. The predominant start site for transcription was identified by primer extension and S1 nuclease analyses to be 50 bases upstream of the ATG initiation codon. Based on the location of the major transcription start site, the functional TATA box is located 29 nucleotides upstream. Putative response elements for AP-2, cAMP, OCT-1, C/EBP, estrogen, glucocorticoids, sterols and thyroid hormone were located in this gene. Also a putative liver-specific element for apolipoproteins, C3P, was identified.
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PMID:Isolation and characterization of clones for the rat hepatic lipase gene upstream regulatory region. 232 83

Extracellular lipase synthesis by Streptomyces lividans 66 carrying the cloned lipase gene (lipA) from Streptomyces exfoliatus M11 was found to be growth phase dependent, since lipase was secreted into the medium mainly during the stationary phase; S1 nuclease protection experiments revealed abundant lipA transcripts in RNA preparations obtained during the stationary phase but not in those obtained during exponential growth. Transcription from the lipA promoter was dependent on the presence of lipR, a contiguous downstream gene with a very high guanine-plus-cytosine content (80.2%). The deduced lipR product consists of a protein of 934 amino acids that shows similarity to known transcriptional activators and has a strong helix-turn-helix motif at its C terminus; this motif is part of a domain homologous to DNA-binding domains of bacterial regulators of the UhpA/LuxR superfamily. The lipR sequence revealed the presence of a leucine residue, encoded by the rare TTA codon, which caused bldA dependence of lipA transcription in Streptomyces coelicolor A3(2); replacement of the TTA codon by the alternate CTC leucine codon alleviated bidA dependence but not the apparent growth phase-dependent regulation of lipA transcription. When lipR expression was induced in a controlled fashion during the exponential growth phase, by placing it under the inducible tipA promoter, lipase synthesis was shifted to the exponential growth phase, indicating that the timing of lipR expression, and not its bldA dependence, is the main cause for stationary-phase transcription of lipA.
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PMID:bldA-dependent expression of the Streptomyces exfoliatus M11 lipase gene (lipA) is mediated by the product of a contiguous gene, lipR, encoding a putative transcriptional activator. 940 Oct 43

Lysosomal acid lipase (LAL) is required for the hydrolysis of intracellular cholesteryl esters and triglycerides that are delivered to lysosomes by low density lipoprotein (LDL) receptor-mediated endocytosis. To understand that the expression of LAL mRNA and protein is tissue and cell specifically regulated in mice, genomic clones for the mouse lysosomal acid lipase (mLAL) gene were isolated and characterized. The 6.8 kb of the mLAL gene 5'-flanking region was sequenced. Comparisons of mouse and human LAL genes organization revealed identical intron/exon boundaries, except for intron 1 of the mouse gene, and identical exonic length of exons 3-9. The transcription start sites and exon 1 of mLAL were characterized by 5'-RACE-PCR and S1 nuclease mapping. Transfection of 5' flanking deletions of mLAL luciferase reporter gene construct identified positive and negative regulatory elements that varied with cell type. Transfection of three progressively smaller pieces of intron 1 inserted into an SV40 promoter and luciferase reporter gene revealed an enhancer-like activity in intron 1 that is also cell type specific. These studies provide insight into the basis for regulation of this critical enzyme in lipid metabolism.
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PMID:Mouse lysosomal acid lipase: characterization of the gene and analysis of promoter activity. 952 82

Extracellular protease and lipase production by psychrotrophic strains of Pseudomonas fluorescens is repressed by iron and regulated by temperature. The regulation of protease and lipase has been investigated in P. fluorescens B52. Whereas lipase production is increased below the optimum growth temperature ('low-temperature regulation'), protease production was relatively constant and only decreased above the optimum growth temperature. The genes encoding protease (aprX) and lipase (lipA) are encoded at opposite ends of a contiguous set of genes which also includes protease inhibitor, Type I secretion functions and two autotransporter proteins. Evidence is presented indicating that these genes constitute an operon, with a promoter adjacent to aprX which has been identified by S1 nuclease analysis. The regulation of aprX and lipA has been investigated at the RNA level and using lacZ fusion strains. Whereas the data are consistent with iron regulation at the transcriptional level, a lipA'-'lacZ fusion is not regulated by temperature, suggesting that temperature regulation is post-transcriptional or post-translational. The possibility of regulation at the level of mRNA decay is discussed.
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PMID:The aprX-lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production. 1115 51