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)

The mouse myelin proteolipid protein (PLP) gene has been studied in normal and jimpymsd mice. Potential upstream regulatory regions of the normal gene have been cloned and mapped, but when these regions were studied in jimpymsd mice by Southern blots, no alterations were observed, relative to the normal gene. To assess whether the low ratio of PLP to DM20 proteins in this mutant reflected an altered PLP/DM20 ratio mRNAs, S1 nuclease analyses were undertaken, which demonstrated that at all ages studied in both jimpy and jimpymsd mice, PLP mRNA was elevated above DM20 mRNA. When exon 3 (the site of the alternative splice signal for DM20 mRNA) of the jimpymsd PLP gene was sequenced, no mutation was identified. The transcription of the PLP gene in normal and mutant animals was studied. The transcription rate increases in normal animals with development, and in very young jimpymsd or jimpy mice, the transcription rate of the PLP gene was close to that of age-matched normal animals. However, by 10 days of age, the transcription rate of this gene in both mutants was significantly below that of age-matched controls. The transcription rate of the myelin basic protein (MBP) gene was also reduced, indicating that expression of both genes is affected by this mutation. In contrast, the transcription rate of the glycerol phosphate dehydrogenase (GPDH) gene, an early marker of oligodendrocytes, is equal to or greater than normal in both mutants. We have confirmed an earlier report of a point mutation in exon 6 of the jimpymsd PLP gene, which converts an alanine to a valine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Mutations in the myelin proteolipid protein gene alter oligodendrocyte gene expression in jimpy and jimpymsd mice. 170 30

The entire glycerol utilization (gylABX) operon of Streptomyces coelicolor A3(2) was cloned and its transcriptional organization and regulation was analyzed by Northern blotting, S1 nuclease mapping and transcriptional fusions. Transcription of the operon is glycerol-inducible and glucose-repressible; glyA (presumptively encoding glycerol kinase), gylB (encoding sn-glycerol-3-phosphate dehydrogenase) and gylX (a non-essential 1.1 kb sequence) are transcribed consecutively to give a 5.4 kb mRNA. Two alternative transcription termination or gyl mRNA processing sites are located within the operon; one (a discrete site) lies between gylB and gylX and the other (a heterogeneous site) positioned 3 kb into the operon, may correspond to the gylA-gylB intercistronic region. A 0.9 kb glycerol-inducible transcription unit is located immediately upstream of gylABX. Transcriptional fusion studies employing an attP site-deleted phage vector provided complementary evidence for the organization of the operon.
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PMID:Cloning and transcription analysis of the entire glycerol utilization (gylABX) operon of Streptomyces coelicolor A3(2) and identification of a closely associated transcription unit. 244 98

We have isolated from a BALB/c genomic library a 17.5-kilobase (kb) DNA fragment containing the entire mouse sn-glycerol-3-phosphate dehydrogenase (glycerol-P dehydrogenase) gene, and a substantial portion of the flanking regions. The DNA sequence of 10.8 kb of this fragment was determined. Using this information, together with the DNA sequence of several partial glycerol-P dehydrogenase cDNA clones and the rabbit glycerol-P dehydrogenase amino acid sequence, we determined the structural organization of the mouse glycerol-P dehydrogenase gene. The gene is 7.3 kb long and contains 8 exons. Transcription starts 19 base pairs 5' of the ATG initiation codon. Sequence analysis and S1 nuclease mapping indicated that the 8th exon contains coding sequences for the last 31 amino acids of glycerol-P-dehydrogenase, followed by 1.7 kb of 3' untranslated mRNA sequence. The mouse glycerol-P dehydrogenase amino acid sequence determined from the DNA sequence is 90% homologous with the rabbit enzyme. An examination of the exon/intron organization of the mouse glycerol-P dehydrogenase gene shows that intron 3 precisely separates the NAD-binding and the catalytic domains and intron 2 separates the adenine- and nicotinamide-binding regions.
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PMID:Primary structure of the mouse glycerol-3-phosphate dehydrogenase gene. 375 21