Interacting Gene-Enzyme Systems in Drosophila

MacIntyre, Ross J.; O’Brien, Stephen J.

doi:10.1146/annurev.ge.10.120176.001433

Cited by 49 publications

(9 citation statements)

References 104 publications

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“…But there is a clue to discriminate primary (or more direct) effect of the mutation from the secondary ones. In Drosophila, studies on structural genes of many enzymes using various deletions and duplications showed that the amount of each gene product is generally proportionate to its gene dosage (MacIntire and O'Brien 1976). In the case of X-chromosome, each X-chromosome in female produces half the amount of products as that of a single male X-chromosome, so that total amount of each X-linked gene product is almost equal in both sexes muscle mutant wings-up B 63…”

Section: Discussionmentioning

confidence: 99%

Electron microscopic and electrophoretic studies of a Drosophila muscle mutant wings-up B.

Mogami

Nonomura

Hotta

1981

The Japanese journal of genetics

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Electron microscopy revealed that, although both thick and thin filaments are present, Z-band and myofibrillar organization are totally lost in indirect flight muscle (IFM) of a Drosophila muscle mutant wings-up B (wup B). The Z-band deficiency correlates well with the gene dosage; in wup B/wup B+ heterozygotes, normal internal structure of the Z-band is restricted only within the central core of the myofibrils. Two-dimensional gel electrophoresis (0'Farrell 1975) revealed that nine myofibrillar proteins are either absent or reduced in the indirect flight muscle of the mutant.Some of the anomalies are not restored in heterozygotes.These observations suggest a possibility that the product of wup B+ gene is one of the Z-band components, without which the regular arrangement of thick and thin filaments cannot be maintained. Possible mechanisms for the fact that a single mutation causes multiple changes on the gel are discussed. We concluded that absence of one component causes disappearance or reduction of others which are functionally and/or structurally related.

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Section: Discussionmentioning

confidence: 99%

Electron microscopic and electrophoretic studies of a Drosophila muscle mutant wings-up B.

Mogami

Nonomura

Hotta

1981

The Japanese journal of genetics

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“…Alternatively, it could be due to an abnormal molecule produced by the mutated gene. To test this, a gene-dosage analysis was done based on the observation that, generally in Drosophila, the amount of gene product is proportional to the number of copies of a gene (19 creating an animal that has a normal complement of the Sh' gene in addition to the mutant Sh gene. If the Sh mutation encodes an altered gene product, the defect should still be present, albeit reduced.…”

Section: Methodsmentioning

confidence: 99%

Abnormal action potentials associated with the Shaker complex locus of Drosophila

Tanouye

Ferrús

Fujita

1981

Proc. Natl. Acad. Sci. U.S.A.

155

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Intracellular recordings ofaction potentials were made from the cervical giant axon in Shaker (Sh) mutants and normal Drosophila. The mutants showed abnormally long delays in repolarization. The defect is not due to abnormal Ca2+ channels, because it persists in the presence of Co2+, blocker. On the other hand, the K+-channel blocker 4-aminopyridine causes a similar effect in normal animals, suggesting that the

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“…We chose to initiate our explorations for peroxisomal mutants in Drosophila by comparing wild-type Oregon R strain flies with the rosy-506 eye-color mutant, in which 90% of the structural gene for xanthine dehydrogenase (xanthine: NAD+ oxidoreductase, EC 1.1.1.204) is deleted (5,6). This protein is a bifunctional oxidoreductase that can act as a dehydrogenase or as an oxidase (xanthine:oxygen oxidoreductase, EC 1.1.3.22) depending upon substrate and acceptor availability (7,8).…”

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Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

Beard

Holtzman

1987

Proc. Natl. Acad. Sci. U.S.A.

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This study shows that peroxisomes are abundant in the Malpighian tubule and gut of wild-type Oregon R Drosophila melanogaster and that the peroxisomal population of the rosy-506 eye-color mutant differs from that of the wild type. Catalase activity in wild-type flies is demonstrable in bodies of appearance and centrifugal behavior comparable to the perixosomes of vertebrate tissues. Xanthine oxidase (xanthine:oxygen oxidoreductase, EC 1. Deficits in one or more of the peroxisomal enzymes and possible defects in peroxisomal structure are correlated with certain human inherited metabolic diseases (1-4). These diseases are still poorly understood, in part because different tissues show different effects of the mutation and in part because alterations in single genes can seemingly have multiple effects on the peroxisomes. Studies of the disorders are made difficult by their rareness and by the obvious limits of working with human material. It would be helpful to study analogues of the disorders in animals amenable to detailed analysis, but thus far such analogues have not been available. We chose to initiate our explorations for peroxisomal mutants in Drosophila by comparing wild-type Oregon R strain flies with the rosy-506 eye-color mutant, in which 90% of the structural gene for xanthine dehydrogenase (xanthine: NAD+ oxidoreductase, EC 1.1.1.204) is deleted (5, 6). This protein is a bifunctional oxidoreductase that can act as a dehydrogenase or as an oxidase (xanthine:oxygen oxidoreductase, EC 1.1.3.22) depending upon substrate and acceptor availability (7,8). The oxidase activity of the enzyme is critical to the degradation of purines in many organisms; the dehydrogenase function is central to the formation of pterinebased eye-color pigments in Drosophila. We suspected that this protein might be peroxisomal because (i) when acting as an oxidase, it produces hydrogen peroxide, a common feature of peroxisomal oxidases; (ii) it requires flavin in generating peroxide, as is found for many other peroxisomal oxidases; and (iii) its role in punine degradation is potentially functionally linked to activity of allantoicase and uricase, known peroxisomal enzymes (9). The subcellular localization of xanthine oxidase is not clearly established. Some cell fractionation studies show most of the enzyme to be soluble (9, 10), while other investigations report some xanthine oxidase cosedimenting with peroxisomal enzymes (11, 12).The study reported here identifies peroxisomes in the Malpighian tubule and gut of adult Drosophila wild-type Oregon R and rosy-506 strains, by virtue of their content of catalase, the peroxisomal "marker" enzyme. To localize xanthine oxidase, we have adapted cytochemical methods used to demonstrate other oxidases. With these methods, we have shown the presence of xanthine oxidase in peroxisomes of wild-type flies and the absence of this enzyme in rosy-506 flies. We also find signs that, as in the human mutations, a relatively simple genetic change can have complex effects on the peroxisomes. Prel...

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Interacting Gene-Enzyme Systems in Drosophila

Cited by 49 publications

References 104 publications

Electron microscopic and electrophoretic studies of a Drosophila muscle mutant wings-up B.

Electron microscopic and electrophoretic studies of a Drosophila muscle mutant wings-up B.

Abnormal action potentials associated with the Shaker complex locus of Drosophila

Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

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