The ?-glycerophosphate dehydrogenase (?-gpdh) polymorphism in Drosophila melanogaster: adult survival under temperature stress

1979 ◽  
Vol 54 (5) ◽  
pp. 235-237 ◽  
Author(s):  
Evelyn Schenfeld ◽  
S. W. McKechnie
Genetics ◽  
1978 ◽  
Vol 90 (1) ◽  
pp. 161-191
Author(s):  
W van Delden ◽  
A C Boerema ◽  
A Kamping

ABSTRACT The allozyme polymorphism at the alcohol dehydrogenase locus in Drosophila melanogaster was studied in order to obtain experimental evidence about the maintenance of this polymorphism. Populations started with different initial allele frequencies from homozygous F and S lines showed a convergence of frequencies on regular food at 25°, leading to values equal to those in the base populations. These results were interpreted as due to some kind of balancing selection. In populations kept at 29.8°, a lower equilibrium F frequency was attained. Addition of ethanol and some other alcohols to the food gave a rapid increase in F frequency, and high humidity decreased the F frequency slightly. Combination or alternation of ethanol and high humidity had variable effects in the populations tested. For a further analysis of the allele-frequency changes, estimates were obtained for egg-to-adult survival under different conditions and for adult survival on ethanol-supplemented food. On ethanol food (both at regular and high humidity), egg-to-adult survival of SS homozygotes was considerably lower than that of the FF and FS genotypes. Under regular conditions of food, temperature and humidity, a tendency to heterozygote superiority was observed, while at high humidity a relative high survival of SS was noticed in some tests. Adult survival of SS was lower than that of FF, but FS was generally intermediate, though the degree of dominance differed between populations. The results are consistent with the hypothesis of the occurrence of selection at the Adh locus.


1977 ◽  
Vol 25 (4) ◽  
pp. 693 ◽  
Author(s):  
PA Parsons

Populations of D. melanogaster and D. simulans were tested for resistance to the cold-temperature stress of - 1�C. Mean mortalities after 48 h followed the sequence D. melanogaster (Townsville) > D. simulans (Townsville) > D. simulans (Melbourne), which were all considerably greater than D. melanogaster (Melbourne). These differences can be related to differences between the sub- tropical climate of Townsville and the temperate climate of Melbourne. The physiological (and genetic) bases of resistance to cold temperature and desiccation differ considerably. The simultaneous genetic study of both traits would be advantageous in understanding the distribution and abundance of natural populations of Drosophila.


Genetics ◽  
1988 ◽  
Vol 120 (3) ◽  
pp. 755-766
Author(s):  
M B Davis ◽  
R J MacIntyre

Abstract The gene for alpha-glycerophosphate oxidase, the nuclear encoded mitochondrial enzyme of the alpha-glycerophosphate cycle (alpha GP); has been mapped in Drosophila melanogaster. Several interstitial deficiencies in region 50c-53AB of chromosome 2R were used to localize the structural gene to 52D2-5. In addition, mutations of alpha GPO were generated; alpha GPO mutants are viable yet flightless. Interactions of alpha GPO with alpha-glycerophosphate dehydrogenase (alpha GPDH), the cytoplasmic enzyme of the alpha GP cycle, were investigated through the synthesis of a series of alpha GPDHnull-alpha GPOnull double mutants. Of the six double null mutants constructed, four alpha GPDH-alpha GPO double nulls are viable and flightless. Two double mutants, however, exhibit an allelic-dependent synthetic lethal phenotype.


Genetics ◽  
1983 ◽  
Vol 105 (2) ◽  
pp. 371-386
Author(s):  
Michael A Kotarski ◽  
Sally Pickert ◽  
Ross J MacIntyre

ABSTRACT The chromosomal region surrounding the structural gene for α-glycerophosphate dehydrogenase (αGpdh, 2-20.5) of Drosophila melanogaster has been studied in detail. Forty-three EMS-induced recessive lethal mutations and five previously identified visible mutations have been localized within the 25A-27D region of chromosome 2 by deficiency mapping and in some cases by a recombination analysis. The 43 lethal mutations specify 17 lethal loci. ?Gpdh has been localized to a single polytene chromosome band, 25F5, and there apparently are no lethals that map to the αGpdh locus.


2016 ◽  
Vol 29 (5) ◽  
pp. 1030-1044 ◽  
Author(s):  
A. Fournier-Level ◽  
A. Neumann-Mondlak ◽  
R. T. Good ◽  
L. M. Green ◽  
J. M. Schmidt ◽  
...  

Genetics ◽  
1972 ◽  
Vol 71 (1) ◽  
pp. 127-138
Author(s):  
Stephen J O'Brien ◽  
Ross J Macintyre

ABSTRACT Seven alleles of the α-Glycerophosphate dehydrogenase-1 (αGpdh-1) locus of Drosophila melanogaster have been described. These include two naturally occurring electrophoretic variants, one EMS-induced electrophoretic variant, and four EMS-induced "null" or "zero" mutants. With the electrophoretic variants, the locus was mapped to II-20.5 ± 2.5. A complementation matrix was prepared utilizing the null mutants. Three of the four mutants and a deletion of the locus (Grell 1967) exhibit dosage dependency. The dosage independent mutant exhibits complementation with two of the other null alleles. Flies genetically deficient in α-glycerophosphate dehydrogenase are fertile, but their relative viability is severely diminished. Such flies also lose the ability to sustain flight, an observation consistent with the enzyme's function in energy production. The levels of mitochondrial α-glycerophosphate oxidase, measured in flies genetically deficient in the cytoplasmic enzyme, were normal.


Genetics ◽  
1983 ◽  
Vol 105 (1) ◽  
pp. 55-69
Author(s):  
Joseph J King ◽  
John F McDonald

ABSTRACT A region-specific, trans-acting regulatory gene that alters in vivo protein levels of α-glycerophosphate dehydrogenase (α-GPDH) has been mapped to position 55.4 on the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of α-GPDH in adult thoracic tissue but has no effect on α-GPDH levels in the abdomen. Although no other thoracic proteins were found to be influenced by the locus, it appears to modify the level of one additional abdominal protein. The action of the gene over development and its possible mode of control are discussed.


Heredity ◽  
1992 ◽  
Vol 68 (4) ◽  
pp. 289-297 ◽  
Author(s):  
L Oudman ◽  
W van Delden ◽  
A Kamping ◽  
R Bijlsma

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