scholarly journals A highly pleiotropic amino acid polymorphism in theDrosophilainsulin receptor contributes to life-history adaptation

Evolution ◽  
2014 ◽  
Vol 68 (12) ◽  
pp. 3395-3409 ◽  
Author(s):  
Annalise B. Paaby ◽  
Alan O. Bergland ◽  
Emily L. Behrman ◽  
Paul S. Schmidt
Keyword(s):  
Life History ◽  
Amino Acid ◽  
Amino Acid Polymorphism

scholarly journals An amino acid polymorphism in theDrosophilainsulin receptor demonstrates pleiotropic and adaptive function in life history traits

2014 ◽  
Author(s):  
Annalise B. Paaby ◽  
Alan O. Bergland ◽  
Emily L. Behrman ◽  
Paul S. Schmidt
Keyword(s):  
Life History ◽  
Amino Acid ◽  
Insulin Signaling ◽  
Evolutionary Biology ◽  
Life History Variation ◽  
Amino Acid Polymorphism ◽  
The North ◽  
Functional Regions ◽  
Climatic Environment ◽  
Life History Tradeoffs

Finding the specific nucleotides that underlie adaptive variation is a major goal in evolutionary biology, but polygenic traits pose a challenge because the complex genotype-phenotype relationship can obscure the effects of individual alleles. However, natural selection working in large wild populations can shift allele frequencies and indicate functional regions of the genome. Previously, we showed that the two most common alleles of a complex amino acid insertion-deletion polymorphism in theDrosophilainsulin receptor show independent, parallel clines in frequency across the North American and Australian continents. Here, we report that the cline is stable over at least a five-year period and that the polymorphism also demonstrates temporal shifts in allele frequency concurrent with seasonal change. We tested the alleles for effects on levels of insulin signaling, fecundity, development time, body size, stress tolerance, and lifespan. We find that the alleles are associated with predictable differences in these traits, consistent with patterns ofDrosophilalife history variation across geography that likely reflect adaptation to the heterogeneous climatic environment. These results implicate insulin signaling as a major mediator of life history adaptation inDrosophila, and suggest that life history tradeoffs can be explained by extensive pleiotropy at a single locus.

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

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 1964-1969 ◽  
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.

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

Blood ◽  
1991 ◽  
Vol 78 (3) ◽  
pp. 681-687 ◽  
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.

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

2008 ◽  
Vol 105 (42) ◽  
pp. 16207-16211 ◽  
Author(s):  
P. S. Schmidt ◽  
C.-T. Zhu ◽  
J. Das ◽  
M. Batavia ◽  
L. Yang ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Polymorphism ◽  
Climatic Adaptation

Serine/alanine amino acid polymorphism of the L-cone photopigment assessed by dual Rayleigh-type color matches

1994 ◽  
Vol 34 (3) ◽  
pp. 377-382 ◽  
Author(s):  
Elizabeth Sanocki ◽  
Steven K. Shevell ◽  
Joris Winderickx
Keyword(s):  
Amino Acid ◽  
Amino Acid Polymorphism

scholarly journals A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
David Roy ◽  
Taryn B. T. Athey ◽  
Jean-Philippe Auger ◽  
Guillaume Goyette-Desjardins ◽  
Marie-Rose Van Calsteren ◽  
...  
Keyword(s):  
Amino Acid ◽  
Streptococcus Suis ◽  
Single Amino Acid ◽  
Amino Acid Polymorphism ◽  
Single Amino Acid Polymorphism

A Phenylalanine Hydroxylase Amino Acid Polymorphism with Implications for Molecular Diagnostics

2001 ◽  
Vol 73 (3) ◽  
pp. 280-284 ◽  
Author(s):  
Torben Gjetting ◽  
Anne Romstad ◽  
Jan Haavik ◽  
Per M. Knappskog ◽  
Angelina X. Acosta ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Diagnostics ◽  
Phenylalanine Hydroxylase ◽  
Amino Acid Polymorphism
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