An amino acid polymorphism in the couch potato gene forms the basis for climatic adaptation in Drosophila melanogaster

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.

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Extensive Amino Acid Polymorphism at the Pgm Locus Is Consistent With Adaptive Protein Evolution in Drosophila melanogaster

Genetics ◽

10.1093/genetics/156.4.1737 ◽

2000 ◽

Vol 156 (4) ◽

pp. 1737-1752 ◽

Cited By ~ 6

Author(s):

Brian C Verrelli ◽

Walter F Eanes

Keyword(s):

Drosophila Melanogaster ◽

Amino Acid ◽

Protein Evolution ◽

Branch Point ◽

Glycogen Metabolism ◽

Strong Linkage Disequilibrium ◽

Amino Acid Polymorphism ◽

Specific Amino Acid ◽

Functional Studies ◽

Latitudinal Clines

Abstract PGM plays a central role in the glycolytic pathway at the branch point leading to glycogen metabolism and is highly polymorphic in allozyme studies of many species. We have characterized the nucleotide diversity across the Pgm gene in Drosophila melanogaster and D. simulans to investigate the role that protein polymorphism plays at this crucial metabolic branch point shared with several other enzymes. Although D. melanogaster and D. simulans share common allozyme mobility alleles, we find these allozymes are the result of many different amino acid changes at the nucleotide level. In addition, specific allozyme classes within species contain several amino acid changes, which may explain the absence of latitudinal clines for PGM allozyme alleles, the lack of association of PGM allozymes with the cosmopolitan In(3L)P inversion, and the failure to detect differences between PGM allozymes in functional studies. We find a significant excess of amino acid polymorphisms within D. melanogaster when compared to the complete absence of fixed replacements with D. simulans. There is also strong linkage disequilibrium across the 2354 bp of the Pgm locus, which may be explained by a specific amino acid haplotype that is high in frequency yet contains an excess of singleton polymorphisms. Like G6pd, Pgm shows strong evidence for a branch point enzyme that exhibits adaptive protein evolution.

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Historical Selection, Amino Acid Polymorphism and Lineage-Specific Divergence at the G6pd Locus in Drosophila melanogaster and D. simulans

Genetics ◽

10.1093/genetics/144.3.1027 ◽

1996 ◽

Vol 144 (3) ◽

pp. 1027-1041 ◽

Cited By ~ 1

Author(s):

Walter F Eanes ◽

Michele Kirchner ◽

Jeanne Yoon ◽

Christiane H Biermann ◽

Ing-Nang Wang ◽

...

Keyword(s):

Drosophila Melanogaster ◽

Amino Acid ◽

Nucleotide Diversity ◽

Amino Acid Replacement ◽

Strong Linkage Disequilibrium ◽

Amino Acid Polymorphism ◽

Interspecific Differences ◽

G6pd Gene ◽

The Common ◽

Species Specific

Abstract The nucleotide diversity across 1705 bp of the G6pd gene is studied in 50 Drosophila melanogaster and 12 D. simulans lines. Our earlier report contrasted intraspecific polymorphism and interspecific differences at silent and replacement sites in these species. This report expands the number of European and African lines and examines the pattern of polymorphism with respect to the common A/B allozymes. In D. melanogaster the silent nucleotide diversity varies 2.8-fold across localities. The B allele sequences are two- to fourfold more variable than the derived A allele, and differences between allozymes are twice as among B alleles. There is strong linkage disequilibrium across the G6pd region. In both species the level of silent polymorphism increases from the 5′ to 3′ ends, while there is no comparable pattern in level of silent site divergence or fixation. The neutral model is not rejected in either species. Using D. yakuba as an outgroup, the D. melanogaster lineage shows a twofold greater rate of silent fixation, but less than half the rate of amino acid replacement. Lineage-specific differences in mutation fixation are inconsistent with neutral expectations and suggest the interaction of species-specific population size differences with both weakly advantageous and deleterious selection.

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Relationship of HDL and coronary heart disease to a common amino acid polymorphism in the cholesteryl ester transfer protein in men with and without hypertriglyceridemia

The Journal of Lipid Research ◽

10.1016/s0022-2275(20)33876-1 ◽

1998 ◽

Vol 39 (5) ◽

pp. 1071-1078 ◽

Cited By ~ 7

Author(s):

Can Bruce ◽

Dan S. Sharp ◽

Alan R. Tall

Keyword(s):

Coronary Heart Disease ◽

Heart Disease ◽

Amino Acid ◽

Cholesteryl Ester ◽

Cholesteryl Ester Transfer Protein ◽

Amino Acid Polymorphism ◽

Common Amino Acid ◽

Transfer Protein ◽

Relationship Of

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Insulin Sensitivity and Body Weight Changes in Young White Carriers of the Codon 64 Amino Acid Polymorphism of the 3-Adrenergic Receptor Gene

Diabetes ◽

10.2337/diab.45.8.1115 ◽

1996 ◽

Vol 45 (8) ◽

pp. 1115-1120 ◽

Cited By ~ 51

Author(s):

S. A. Urhammer ◽

J. O. Clausen ◽

T. Hansen ◽

O. Pedersen

Keyword(s):

Body Weight ◽

Amino Acid ◽

Insulin Sensitivity ◽

Adrenergic Receptor ◽

Receptor Gene ◽

Weight Changes ◽

Amino Acid Polymorphism ◽

Body Weight Changes ◽

Adrenergic Receptor Gene

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GEOGRAPHIC VARIATION IN DIAPAUSE INCIDENCE, LIFE-HISTORY TRAITS, AND CLIMATIC ADAPTATION IN DROSOPHILA MELANOGASTER

Evolution ◽

10.1554/05-115.1 ◽

2005 ◽

Vol 59 (8) ◽

pp. 1721 ◽

Cited By ~ 40

Author(s):

Paul S. Schmidt ◽

Luciano Matzkin ◽

Michael Ippolito ◽

Walter F. Eanes

Keyword(s):

Drosophila Melanogaster ◽

Life History ◽

Geographic Variation ◽

Life History Traits ◽

Climatic Adaptation ◽

Diapause Incidence

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The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster

Biochemical Journal ◽

10.1042/bj1870875 ◽

1980 ◽

Vol 187 (3) ◽

pp. 875-883 ◽

Cited By ~ 135

Author(s):

D R Thatcher

Keyword(s):

Drosophila Melanogaster ◽

Amino Acid ◽

Amino Acid Sequence ◽

Alcohol Dehydrogenase ◽

Aspartic Acid ◽

Structure Prediction ◽

Secondary Structure Prediction ◽

British Library ◽

Horse Liver ◽

And Staphylococcus Aureus

The sequence of three alcohol dehydrogenase alleloenzymes from the fruitfly Drosophila melanogaster has been determined by the sequencing of peptides produced by trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus-V8-proteinase digestion. The amino acid sequence shows no obvious homology with the published sequences of the horse liver and yeast enzymes, and secondary structure prediction suggests that the nucleotide-binding domain is located in the N-terminal half of the molecule. The amino acid substitutions between AdhN-11 (a point mutation of AdhF), AdhS and AdhUF alleloenzymes were identified. AdhN-11 alcohol dehydrogenase differed from the other two by a glycine-14-(AdhS and AdhUF)-to-aspartic acid substitution, the AdhS enzyme from AdhN-11 and AdhUF enzymes by a threonine-192-(AdhN-11 and AdhUF)-to-lysine (AdhS) substitution and the AdhUF enzyme was found to differ by an alanine-45-(AdhS and AdhN-11)-to-aspartic acid (AdhUF) charge substitution and a ‘silent’ asparagine-8-(AdhS and AdhN-11)-to-alanine (AdhUF) substitution. Detailed sequence evidence has been deposited as Supplementary Publication SUP 50107 (36 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

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S elements: a family of Tc1-like transposons in the genome of Drosophila melanogaster.

Genetics ◽

10.1093/genetics/141.4.1425 ◽

1995 ◽

Vol 141 (4) ◽

pp. 1425-1438 ◽

Cited By ~ 1

Author(s):

P J Merriman ◽

C D Grimes ◽

J Ambroziak ◽

D A Hackett ◽

P Skinner ◽

...

Keyword(s):

Drosophila Melanogaster ◽

Amino Acid ◽

Transposable Elements ◽

Sibling Species ◽

Inverted Repeat ◽

Open Reading Frame ◽

Drosophila Species ◽

Insertion Mutation ◽

Reading Frame ◽

Diploid Genome

Abstract The S elements form a diverse family of long-inverted-repeat transposons within the genome of Drosophila melanogaster. These elements vary in size and sequence, the longest consisting of 1736 bp with 234-bp inverted terminal repeats. The longest open reading frame in an intact S element could encode a 345-amino acid polypeptide. This polypeptide is homologous to the transposases of the mariner-Tc1 superfamily of transposable elements. S elements are ubiquitous in D. melanogaster populations and also appear to be present in the genomes of two sibling species; however, they seem to be absent from 17 other Drosophila species that were examined. Within D. melanogaster strains, there are, on average, 37.4 cytologically detectable S elements per diploid genome. These elements are scattered throughout the chromosomes, but several sites in both the euchromatin and beta heterochromatin are consistently occupied. The discovery of an S-element-insertion mutation and a reversion of this mutation indicates that S elements are at least occasionally mobile in the D. melanogaster genome. These elements seem to insert at an AT dinucleotide within a short palindrome and apparently duplicate that dinucleotide upon insertion.

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A 13-mer peptide straddling the leucine33/proline33 polymorphism in glycoprotein IIIa does not define the PLA1 epitope

Blood ◽

10.1182/blood.v77.9.1964.1964 ◽

1991 ◽

Vol 77 (9) ◽

pp. 1964-1969 ◽

Cited By ~ 22

Author(s):

F Flug ◽

R Espinola ◽

LX Liu ◽

C SinQuee ◽

R DaRosso ◽

...

Keyword(s):

Amino Acid ◽

Polyclonal Antibodies ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Adenosine Diphosphate ◽

Enzyme Linked Immunosorbent Assay ◽

Amino Acid Polymorphism ◽

Glycoprotein Iiia ◽

Polymerase Chain ◽

Induced Aggregation

Abstract We confirm the recent report (J Clin Invest 83:1778, 1989) of a polymorphism at amino acid 33 of platelet GPIIIa associated with the PLA1/PLA2 phenotype by using the polymerase chain reaction on cDNA derived from platelet RNA, using the base-pair primers 105–129 and 452- 428. Platelet cDNA from three PLA2-homozygous individuals, when digested with Nci I, gave two bands of 256 bp and 91 bp, whereas eight PLA1 cDNAs gave a single band of 347 bp. Two 13-mer amino acid peptides straddling the amino acid polymorphism: SDEALP (L/P) GSPRCD were synthesized for epitope studies. Two mouse polyclonal antibodies were raised: one against the PLA1-associated peptide, the other against the PLA2 peptide. Both antibodies react with either peptide, as well as with both PLA1 and PLA2 platelets. The PLA1 peptide did not block the binding of two different human anti-PLA1 antibodies to the 100-Kd GPIIIa band on immunoblot of platelet extracts; neither did it block the binding of the same antibodies to PLA1-platelet extracts in an enzyme-linked immunosorbent assay. Further studies were performed on the PLA1 epitope following subtilisin digestion of purified GPIIIa. A 55-Kd fragment was obtained that retained the PLA1 epitope as well as the first 13 N-terminal amino acids of GPIIIa. Reduction of the 55-Kd fragment resulted in loss of the PLA1 epitope with production of a 67- Kd, 21-Kd, and 10-Kd band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The 55-Kd band does not react with LK-2, a monoclonal antibody versus GPIIIa that inhibits adenosine diphosphate, collagen, epinephrine, and thrombin-induced aggregation. Thus, the PLA1 epitope is conformation-induced, resides on an N-terminal 55-Kd fragment composed of two or more peptides held together by -SH bonds, and is not required for platelet aggregation.

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Effect of single amino acid substitutions on the formation of the PlA and Bak alloantigenic epitopes

Blood ◽

10.1182/blood.v78.3.681.681 ◽

1991 ◽

Vol 78 (3) ◽

pp. 681-687 ◽

Cited By ~ 51

Author(s):

A Goldberger ◽

M Kolodziej ◽

M Poncz ◽

JS Bennett ◽

PJ Newman

Keyword(s):

Amino Acid ◽

Expression System ◽

Single Amino Acid ◽

Expression Vectors ◽

Membrane Glycoproteins ◽

Amino Acid Polymorphism ◽

Specific Expression ◽

Mammalian Expression ◽

Single Amino Acid Polymorphisms ◽

Necessary And Sufficient

Abstract The subunits that comprise the platelet-specific integrin alpha IIb beta 3 are polymorphic in nature, with several allelic forms present in the human gene pool. Minor changes in the secondary and tertiary structures of platelet membrane glycoproteins (GP) IIb and IIIa encoded by these alleles can result in an alloimmune reaction after transfusion or during pregnancy. To better understand the molecular structure of the PlA alloantigen system, located on GPIIIa, and the Bak alloantigen on GPIIb, we used a heterologous mammalian expression system to express these integrin subunits in their known polymorphic forms. An expression vector containing the PlA1 form of a GPIIIa cDNA, which encodes a leucine at amino acid 33 (Leu33), was modified to express the PlA2- associated form encoding a proline at amino acid 33 (Pro33). Similarly, a Baka GPIIb cDNA expressing an isoleucine at amino acid 843 (IIe843) was modified to express the Bakb form containing a serine at the same position (Ser843). Transfection of these vectors into COS cells resulted in the synthesis of GPIIb and GPIIIa molecules that were identical in size to those present in platelet lysates. Immunoprecipitation of the GPIIIa-transfected COS lysates with PlA)- specific alloantisera indicated that the Leu33 form was recognized only by anti-PIA1 sera while the Pro33 form was bound only by anti-PlA2 sera, showing that single amino acid polymorphisms are necessary and sufficient to direct the formation of the PlA1 and PlA2 alloepitopes. Similar experiments with Bak allele-specific expression vectors indicated that while the amino acid polymorphism (IIe843 in equilibrium Ser843) was necessary, posttranslational processing of pro-IIb was required for efficient exposure of both the Baka and Bakb alloepitopes.

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