Inhibition of Female Drosophila melanogaster Remating by a Seminal Fluid Protein (Esterase 6)

Evolution ◽  
1986 ◽  
Vol 40 (5) ◽  
pp. 1084 ◽  
Author(s):  
David Scott
Keyword(s):  
Drosophila Melanogaster ◽  
Seminal Fluid ◽  
Esterase 6 ◽  
Seminal Fluid Protein

Molecular population genetics of structural variants of esterase 6 in Drosophila melanogaster

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 788-796 ◽  
Author(s):  
J. G. Oakeshott ◽  
P. H. Cooke ◽  
R. C. Richmond ◽  
A. Bortoli ◽  
A. Y. Game ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Natural Selection ◽  
Amino Acid ◽  
Seminal Fluid ◽  
Biochemical Properties ◽  
Nucleotide Polymorphisms ◽  
Amino Acid Polymorphism ◽  
Sequence Comparisons ◽  
Esterase 6 ◽  
Latitudinal Clines

Several lines of evidence indicate that natural selection operates between the major EST6-F and EST6-S allozymes of Drosophila melanogaster. In particular, consistent latitudinal clines and seasonal variation in their relative frequencies strongly suggest that they are not selectively equivalent in field populations. Several laboratory studies have found frequency-dependent fitness differences among the Est6-F and Est6-S genotypes. Moreover, the purified EST6-F and EST6-S allozymes differ in biochemical properties and the physiology of the enzyme, as a major component of the seminal fluid, suggests that these differences could affect reproductive aspects of fitness. However, molecular analyses reveal high levels of variation in the EST6 protein both within and between the EST6-F and EST6-S allozymes. Limited thermostability and more sensitive electrophoretic analyses reveal at least 17 variants of the two allozymes and sequence comparisons among 13 isolates of the Est6 gene reveal 16 nucleotide polymorphisms that would lead to amino acid differences. Two closely linked amino acid differences are strongly associated with the major difference between EST6-F and EST6-S; either or both of these are likely to cause the observed biochemical differences between EST6-F and EST6-S and may be the primary targets for the selection between these allozymes. The functional and adaptive significance of the other amino acid polymorphisms is unclear, although the data suggest that the EST6-8 haplotype within EST6-S has both arisen and proliferated relatively recently.Key words: Drosophila melanogaster, esterase 6, nucleotide and amino acid polymorphism, natural selection.

Localization and longevity of seminal-fluid esterase 6 in mated female Drosophila melanogaster

1990 ◽  
Vol 36 (2) ◽  
pp. 93-101 ◽  
Author(s):  
Douglas B. Meikle ◽  
Kathy B. Sheehan ◽  
Debra M. Phillis ◽  
Rollin C. Richmond
Keyword(s):  
Drosophila Melanogaster ◽  
Seminal Fluid ◽  
Esterase 6 ◽  
Mated Female

scholarly journals Mated Drosophila melanogaster Females Require a Seminal Fluid Protein, Acp36DE, to Store Sperm Efficiently

Genetics ◽  
1999 ◽  
Vol 153 (2) ◽  
pp. 845-857 ◽  
Author(s):  
Deborah M Neubaum ◽  
Mariana F Wolfner
Keyword(s):  
Drosophila Melanogaster ◽  
Seminal Fluid ◽  
Sperm Storage ◽  
Egg Laying ◽  
Limited Area ◽  
Seminal Fluid Proteins ◽  
Barrier Formation ◽  
Storage Organs ◽  
Initial Storage ◽  
Seminal Fluid Protein

Abstract Mated females of many animal species store sperm. Sperm storage profoundly influences the number, timing, and paternity of the female’s progeny. To investigate mechanisms for sperm storage in Drosophila melanogaster, we generated and analyzed mutations in Acp36DE. Acp36DE is a male seminal fluid protein whose localization in mated females suggested a role in sperm storage. We report that male-derived Acp36DE is essential for efficient sperm storage by females. Acp36DE1 (null) mutant males produced and transferred normal amounts of sperm and seminal fluid proteins. However, mates of Acp36DE1 males stored only 15% as many sperm and produced 10% as many adult progeny as control-mated females. Moreover, without Acp36DE, mated females failed to maintain an elevated egg-laying rate and decreased receptivity, behaviors whose persistence (but not initiation) normally depends on the presence of stored sperm. Previous studies suggested that a barrier in the oviduct confines sperm and Acp36DE to a limited area near the storage organs. We show that Acp36DE is not required for barrier formation, but both Acp36DE and the barrier are required for maximal sperm storage. Acp36DE associates tightly with sperm. Our results indicate that Acp36DE is essential for the initial storage of sperm, and that it may also influence the arrangement and retention of stored sperm.

scholarly journals STUDIES OF ESTERASE 6 IN DROSOPHILA MELANOGASTER. VI. EJACULATE COMPETITIVE ABILITIES OF MALES HAVING NULL OR ACTIVE ALLELES

Genetics ◽  
1981 ◽  
Vol 97 (1) ◽  
pp. 85-94 ◽  
Author(s):  
Donald G Gilbert ◽  
Rollin C Richmond
Keyword(s):  
Drosophila Melanogaster ◽  
Sexual Selection ◽  
Competitive Ability ◽  
Seminal Fluid ◽  
Experimental Conditions ◽  
Competition Mechanism ◽  
Esterase 6 ◽  
Significant Difference ◽  
Female Genotype ◽  
Male Genotype

ABSTRACT Recent studies of the function of the polymorphic seminal fluid enzyme, esterase 6, of Drosophila melanogaster suggested that it may act in the process of sperm displacement (Gilbert, Richmond and Sheehan, 1981a). This report examines the competitive ability of ejaculates from males homozygous for null or active alleles of esterase 6 under three experimental conditions that model aspects of sexual selection affecting males. The results demonstrate no significant difference in ejaculate competition between esterase 6 null or active male types, but marker males used for paternity identification had poorly competitive ejaculates. The proportion of second-male progeny, P  2, used as an index of competition is primarily influenced by second-male genotype and uninfluenced by female genotype. P2 can change with time from remating and be unaffected by different intensities of competition, which suggests a complex ejaculate competition mechanism.

scholarly journals Contrasting Histories of Three Gene Regions Associated With In(3L)Payne of Drosophila melanogaster

Genetics ◽  
1996 ◽  
Vol 144 (4) ◽  
pp. 1565-1575 ◽  
Author(s):  
Esteban Hasson ◽  
Walter F Eanes
Keyword(s):  
Drosophila Melanogaster ◽  
Sequence Variation ◽  
Present Report ◽  
Genetic Exchange ◽  
Nucleotide Variation ◽  
Distal Breakpoint ◽  
Esterase 6 ◽  
The Common ◽  
Neutrality Tests ◽  
Hsp83 Gene

In the present report, we studied nucleotide variation in three gene regions of Drosophila melanogaster, spanning >5 kb and showing different degrees of association with the cosmopolitan inversion In(3-L)Payne. The analysis of sequence variation in the regions surrounding the breakpoints and the heat shock 83 (Hsp83) gene locus, located close to the distal breakpoint, revealed the absence of shared polymorphisms and the presence of a number of fixed differences between arrangements, indicating absence of genetic exchange. In contrast, for the esterase-6 gene region, located in the center of the inversion, we observed the presence of shared polymorphisms between arrangements suggesting genetic exchange. In the regions close to the breakpoints, the common St arrangement is 10 times more polymorphic than inverted chromosomes. We propose that the lack of recombination between arrangements in these regions coupled with genetic hitchhiking is the best explanation for the low heterozygosity observed in inverted lines. Using the data for the breakpoints, we estimate that this inversion polymorphism is around 0.36 million yr old. Although it is widely accepted that inversions are examples of balanced polymorphisms, none of the current neutrality tests including our Monte Carlo simulations showed significant departure from neutral expectations.

Phosphoglucomutase (PGM) and Esterase-6 (EST-6) alleles in Drosophila melanogaster: An attempt to detect linkage disequilibrium

Genetica ◽  
1978 ◽  
Vol 49 (2-3) ◽  
pp. 225-227 ◽  
Author(s):  
G. Trippa ◽  
G. A. Danieli ◽  
R. Costa ◽  
R. Scozzari
Keyword(s):  
Drosophila Melanogaster ◽  
Linkage Disequilibrium ◽  
Esterase 6
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