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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 27 (1971), S. 99-100 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Neben zwei elektrophoretisch verschiedenen Varianten derDrosophila-Alkoholdehydrogenase kommen innerhalb dieser Varianten weitere Variationen vor, die sich in ihrer spezifischen Aktivität und Temperaturempfindlichkeit unterscheiden. Es wird daraus geschlossen, dass der Grad des Polymorphismus von Populationen grösser sei, als aufgrund elektrophoretischer Untersuchungen geschätzt wird.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 28 (1990), S. 443-443 
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 22 (1984), S. 153-168 
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; Drosophila ; activity ratio ; specific activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.
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  • 4
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate dehydrogenase ; restriction map ; duplication ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Restriction site variation in a 25-kb region including thesn-glycerol-3-phosphate dehydrogenase (Gpdh) locus has been assessed in 29 single femaleD. melanogaster lines from the Cardwell (Australia, QLD) population. TheGpdh locus was duplicated in about one-third of the lines, although the duplication was incomplete and lacked exons 1 and 2. There was no restriction site variation in the duplicated region. Three insertions were found in the gene region but only one affected GPDH activity. The lines with the duplication had higher levels of GPDH activity and protein amount than did nonduplicated lines. This effect was also observed in lines extracted from two other Australian populations. The duplication is shown to have a similar structure in each population investigated and is also present in populations from China and Africa. It is suggested that the effect of the duplication on GPDH activity, which might be due to structural factors affecting transcription at theGpdh locus, could account for the worldwide distribution of the duplication.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 27 (1989), S. 679-688 
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; null allele ; DNA rearrangement ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract An alcohol dehydrogenase null activity allele,Adh nAH52 , extracted from a natural population ofDrosophila melanogaster has been cloned and sequenced. Compared with the wild-type consensus sequence, the nucleotide sequence ofAdh nAH52 contains eight extra bases in intron 2, adjacent to the 5' splice site. It seems likely that the extra bases result from two structural changes, with a 10-base pair insertion at the same site as a 2-base pair deletion. The insertion includes an 8-base pair duplication of an adjoining region. This structural change alters transcription to give rise to an mRNA which is longer than normal and at 10% of the wild-type level.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 27 (1989), S. 679-688 
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; null allele ; DNA rearrangement ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract An alcohol dehydrogenase null activity allele,Adh nAH52 , extracted from a natural population ofDrosophila melanogaster has been cloned and sequenced. Compared with the wild-type consensus sequence, the nucleotide sequence ofAdh nAH52 contains eight extra bases in intron 2, adjacent to the 5' splice site. It seems likely that the extra bases result from two structural changes, with a 10-base pair insertion at the same site as a 2-base pair deletion. The insertion includes an 8-base pair duplication of an adjoining region. This structural change alters transcription to give rise to an mRNA which is longer than normal and at 10% of the wild-type level.
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  • 7
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate ; dehydrogenase ; low activity ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Northern analyses of two low-activitysn-glycerol-3-phosphate dehydrogenase(Gpdh) alleles extracted from natural populations ofDrosophila melanogaster showed that one of them,Gpdh ACyg22 , produced wild-type levels of a normal sized (1.7-kb) mRNA but the other,Gpdh AMB5 , had very low levels of a 1.7-kb mRNA together with low levels of a transcript 200 bp larger. The two variant genes were cloned and sequenced. Compared with normal activity alleles, there were two nucleotide differences in the DNA sequence ofGpdh ACyg22 which were in first-codon positions and would be expected to give rise to Asn-13 → Tyr and Arg-272 → Cys substitutions. The second of these changes is most likely to account for the altered properties of the enzyme. In contrast, none of the nucleotide differences inGpdh AMB5 would give rise to amino acid substitutions, but a 76-bp deletion in the 5′ region removed the normal TATA box and there was a 20-bp insertion in the same region. One of the two transcripts was derived from the use of a substitute TATA box sequence in the insertion, but the 1.9-kb transcript had heterogeneous 5′ ends that were not associated with substitute TATA box sequences. The two transcripts either are produced at a lower rate or are less stable than the normal mRNA.
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  • 8
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate dehydrogenase ; restriction map ; duplication ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Restriction site variation in a 25-kb region including thesn-glycerol-3-phosphate dehydrogenase (Gpdh) locus has been assessed in 29 single femaleD. melanogaster lines from the Cardwell (Australia, QLD) population. TheGpdh locus was duplicated in about one-third of the lines, although the duplication was incomplete and lacked exons 1 and 2. There was no restriction site variation in the duplicated region. Three insertions were found in the gene region but only one affected GPDH activity. The lines with the duplication had higher levels of GPDH activity and protein amount than did nonduplicated lines. This effect was also observed in lines extracted from two other Australian populations. The duplication is shown to have a similar structure in each population investigated and is also present in populations from China and Africa. It is suggested that the effect of the duplication on GPDH activity, which might be due to structural factors affecting transcription at theGpdh locus, could account for the worldwide distribution of the duplication.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 28 (1990), S. 443-443 
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 36 (1998), S. 329-350 
    ISSN: 1573-4927
    Keywords: DROSOPHILA ; SN-GLYCEROL-3-PHOSPHATE DEHYDROGENASE ; ENHANCER ; GPDH
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract P element-mediated transformation has been usedto investigate the regulation of expression of thesn-glycerol-3-phosphate dehydrogenase gene ofDrosophila melanogaster. A 13-kb constructcontaining the eight exons and associated introns, 5 kb of the5′ region, and 3 kb downstream from the structuralgene produced normal levels of enzyme activity andrescued the poor viability of flies lacking the enzyme. All the regulatory elements essential fornormal enzyme expression were located in a fragment thatincluded the exons and introns and 1-kb upstreamnoncoding sequence. Deletions of the 1.6-kb secondintron reduced activity to 25%. Transformants withfusion constructs between the sn-glycerol-3-phosphatedehydrogenase gene and the beta-galactosidase gene fromE. coli revealed three elements that affectedexpression. A (CT)9 repeat element at the5′ end of the second intron increased expressionin both larvae and adults, particularly at emergence. Asecond regulatory element, which includes a(CT)7 repeat, was located 5′ to the TATA box and had similareffects on the gene's expression. A third, undefined,enhancer was located in the second intron, between 0.5and 1.8 kb downstream of the translation initiationcodon. This element increases enzyme activity to asimilar extent in larvae and adults but has littleeffect when the enhancer at the 5′ end of theintron is present.
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