GEPHE SUMMARY Print
Entry Status
Published
GepheID
GP00000456
Main curator
Martin
PHENOTYPIC CHANGE
Trait Category
Trait State in Taxon A
Peromyscus maniculatus -low elevation
Trait State in Taxon B
Peromyscus maniculatus - high elevation
Ancestral State
Taxon A
Taxonomic Status
Taxon A
Common Name
North American deer mouse
Synonyms
North American deer mouse; Peromyscus maniculatus (Wagner, 1845); MSB Mamm 74965; MSB:collector:Mamm:74965; Peromyscus maniculatis
Rank
species
Lineage
Show more ... eostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Cricetidae; Neotominae; Peromyscus
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Common Name
North American deer mouse
Synonyms
North American deer mouse; Peromyscus maniculatus (Wagner, 1845); MSB Mamm 74965; MSB:collector:Mamm:74965; Peromyscus maniculatis
Rank
species
Lineage
Show more ... eostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Cricetidae; Neotominae; Peromyscus
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Mutation #1
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
His50Pro; Gly57Ala; Ala60Gly; Asp64Gly; Gly71Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid His Pro 50
Authors
Storz JF; Sabatino SJ; Hoffmann FG; Gering EJ; Moriyama H; Ferrand N; Monteiro B; Nachman MW
Abstract
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus alpha-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated alpha-globin genes of P. maniculatus from high- and low-altitude localities (i) to identify the specific mutations that may be responsible for the divergent fine-tuning of hemoglobin function and (ii) to test whether the genes exhibit the expected signature of diversifying selection between populations that inhabit different elevational zones. Results demonstrate that functionally distinct protein alleles are maintained as a long-term balanced polymorphism and that adaptive modifications of hemoglobin function are produced by the independent or joint effects of five amino acid mutations that modulate oxygen-binding affinity.
Mutation #2
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
His50Pro; Gly57Ala; Ala60Gly; Asp64Gly; Gly71Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Gly Ala 57
Authors
Storz JF; Sabatino SJ; Hoffmann FG; Gering EJ; Moriyama H; Ferrand N; Monteiro B; Nachman MW
Abstract
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus alpha-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated alpha-globin genes of P. maniculatus from high- and low-altitude localities (i) to identify the specific mutations that may be responsible for the divergent fine-tuning of hemoglobin function and (ii) to test whether the genes exhibit the expected signature of diversifying selection between populations that inhabit different elevational zones. Results demonstrate that functionally distinct protein alleles are maintained as a long-term balanced polymorphism and that adaptive modifications of hemoglobin function are produced by the independent or joint effects of five amino acid mutations that modulate oxygen-binding affinity.
Mutation #3
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
His50Pro; Gly57Ala; Ala60Gly; Asp64Gly; Gly71Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Ala Gly 60
Authors
Storz JF; Sabatino SJ; Hoffmann FG; Gering EJ; Moriyama H; Ferrand N; Monteiro B; Nachman MW
Abstract
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus alpha-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated alpha-globin genes of P. maniculatus from high- and low-altitude localities (i) to identify the specific mutations that may be responsible for the divergent fine-tuning of hemoglobin function and (ii) to test whether the genes exhibit the expected signature of diversifying selection between populations that inhabit different elevational zones. Results demonstrate that functionally distinct protein alleles are maintained as a long-term balanced polymorphism and that adaptive modifications of hemoglobin function are produced by the independent or joint effects of five amino acid mutations that modulate oxygen-binding affinity.
Mutation #4
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
His50Pro; Gly57Ala; Ala60Gly; Asp64Gly; Gly71Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Asp Gly 64
Authors
Storz JF; Sabatino SJ; Hoffmann FG; Gering EJ; Moriyama H; Ferrand N; Monteiro B; Nachman MW
Abstract
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus alpha-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated alpha-globin genes of P. maniculatus from high- and low-altitude localities (i) to identify the specific mutations that may be responsible for the divergent fine-tuning of hemoglobin function and (ii) to test whether the genes exhibit the expected signature of diversifying selection between populations that inhabit different elevational zones. Results demonstrate that functionally distinct protein alleles are maintained as a long-term balanced polymorphism and that adaptive modifications of hemoglobin function are produced by the independent or joint effects of five amino acid mutations that modulate oxygen-binding affinity.
Mutation #5
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
His50Pro; Gly57Ala; Ala60Gly; Asp64Gly; Gly71Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Gly Ser 71
Authors
Storz JF; Sabatino SJ; Hoffmann FG; Gering EJ; Moriyama H; Ferrand N; Monteiro B; Nachman MW
Abstract
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus alpha-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated alpha-globin genes of P. maniculatus from high- and low-altitude localities (i) to identify the specific mutations that may be responsible for the divergent fine-tuning of hemoglobin function and (ii) to test whether the genes exhibit the expected signature of diversifying selection between populations that inhabit different elevational zones. Results demonstrate that functionally distinct protein alleles are maintained as a long-term balanced polymorphism and that adaptive modifications of hemoglobin function are produced by the independent or joint effects of five amino acid mutations that modulate oxygen-binding affinity.
RELATED GEPHE
Related Haplotypes
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COMMENTS
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