GEPHE SUMMARY Print
Entry Status
Published
GepheID
GP00000477
Main curator
Martin
PHENOTYPIC CHANGE
Trait Category
Trait State in Taxon A
Elephantids
Trait State in Taxon B
Mammuthus primigenius
Ancestral State
Data not curated
Taxonomic Status
Taxon A
Latin Name
Common Name
elephants
Synonyms
elephants
Rank
family
Lineage
Show more ... ia; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Afrotheria; Proboscidea
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Common Name
woolly mammoth
Synonyms
woolly mammoth; mammoth
Rank
species
Lineage
Show more ... ta; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Afrotheria; Proboscidea; Elephantidae; Mammuthus
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Generic Gene Name
HBB
Synonyms
ECYT6; CD113t-C; beta-globin
Sequence Similarities
Belongs to the globin family.
UniProtKB
Homo sapiens
GenebankID or UniProtKB
Mutation #1
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
Thr12Ala
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Thr Ala 12
Authors
Campbell KL; Roberts JE; Watson LN; Stetefeld J; Sloan AM; Signore AV; Howatt JW; Tame JR; et al. ... show more
Abstract
We have genetically retrieved, resurrected and performed detailed structure-function analyses on authentic woolly mammoth hemoglobin to reveal for the first time both the evolutionary origins and the structural underpinnings of a key adaptive physiochemical trait in an extinct species. Hemoglobin binds and carries O(2); however, its ability to offload O(2) to respiring cells is hampered at low temperatures, as heme deoxygenation is inherently endothermic (that is, hemoglobin-O(2) affinity increases as temperature decreases). We identify amino acid substitutions with large phenotypic effect on the chimeric beta/delta-globin subunit of mammoth hemoglobin that provide a unique solution to this problem and thereby minimize energetically costly heat loss. This biochemical specialization may have been involved in the exploitation of high-latitude environments by this African-derived elephantid lineage during the Pleistocene period. This powerful new approach to directly analyze the genetic and structural basis of physiological adaptations in an extinct species adds an important new dimension to the study of natural selection.
Additional References
Mutation #2
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
Ala86Ser
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Ala Ser 86
Authors
Campbell KL; Roberts JE; Watson LN; Stetefeld J; Sloan AM; Signore AV; Howatt JW; Tame JR; et al. ... show more
Abstract
We have genetically retrieved, resurrected and performed detailed structure-function analyses on authentic woolly mammoth hemoglobin to reveal for the first time both the evolutionary origins and the structural underpinnings of a key adaptive physiochemical trait in an extinct species. Hemoglobin binds and carries O(2); however, its ability to offload O(2) to respiring cells is hampered at low temperatures, as heme deoxygenation is inherently endothermic (that is, hemoglobin-O(2) affinity increases as temperature decreases). We identify amino acid substitutions with large phenotypic effect on the chimeric beta/delta-globin subunit of mammoth hemoglobin that provide a unique solution to this problem and thereby minimize energetically costly heat loss. This biochemical specialization may have been involved in the exploitation of high-latitude environments by this African-derived elephantid lineage during the Pleistocene period. This powerful new approach to directly analyze the genetic and structural basis of physiological adaptations in an extinct species adds an important new dimension to the study of natural selection.
Additional References
Mutation #3
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
Glu101Gln
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid Glu Gln 101
Authors
Campbell KL; Roberts JE; Watson LN; Stetefeld J; Sloan AM; Signore AV; Howatt JW; Tame JR; et al. ... show more
Abstract
We have genetically retrieved, resurrected and performed detailed structure-function analyses on authentic woolly mammoth hemoglobin to reveal for the first time both the evolutionary origins and the structural underpinnings of a key adaptive physiochemical trait in an extinct species. Hemoglobin binds and carries O(2); however, its ability to offload O(2) to respiring cells is hampered at low temperatures, as heme deoxygenation is inherently endothermic (that is, hemoglobin-O(2) affinity increases as temperature decreases). We identify amino acid substitutions with large phenotypic effect on the chimeric beta/delta-globin subunit of mammoth hemoglobin that provide a unique solution to this problem and thereby minimize energetically costly heat loss. This biochemical specialization may have been involved in the exploitation of high-latitude environments by this African-derived elephantid lineage during the Pleistocene period. This powerful new approach to directly analyze the genetic and structural basis of physiological adaptations in an extinct species adds an important new dimension to the study of natural selection.
Additional References
RELATED GEPHE
Related Genes
No matches found.
Related Haplotypes
No matches found.
COMMENTS
Needs curation @SeveralMutationsWithEffect
YOUR FEEDBACK is welcome!