Predictable convergence in hemoglobin function has unpredictable molecular underpinnings

Chandrasekhar Natarajan; Federico G Hoffmann; Roy E Weber; Angela Fago; Christopher C Witt; Jay F Storz

doi:10.1126/science.aaf9070

Predictable convergence in hemoglobin function has unpredictable molecular underpinnings

Chandrasekhar Natarajan, Federico G Hoffmann, Roy E Weber, Angela Fago, Christopher C Witt, Jay F Storz

Institut for Biologi - Zoofysiologi

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

173 Citationer (Scopus)

Abstract

To investigate the predictability of genetic adaptation, we examined the molecular basis of convergence in hemoglobin function in comparisons involving 56 avian taxa that have contrasting altitudinal range limits. Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa, but few such changes were attributable to parallel amino acid substitutions at key residues. Thus, predictable changes in biochemical phenotype do not have a predictable molecular basis. Experiments involving resurrected ancestral proteins revealed that historical substitutions have context-dependent effects, indicating that possible adaptive solutions are contingent on prior history. Mutations that produce an adaptive change in one species may represent precluded possibilities in other species because of differences in genetic background.

Originalsprog	Engelsk
Tidsskrift	Science
Vol/bind	354
Nummer	6310
Sider (fra-til)	336-339
Antal sider	4
ISSN	0036-8075
DOI	https://doi.org/10.1126/science.aaf9070
Status	Udgivet - 21 okt. 2016

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10.1126/science.aaf9070

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5464326/pdf/nihms865057.pdf

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abstract = "To investigate the predictability of genetic adaptation, we examined the molecular basis of convergence in hemoglobin function in comparisons involving 56 avian taxa that have contrasting altitudinal range limits. Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa, but few such changes were attributable to parallel amino acid substitutions at key residues. Thus, predictable changes in biochemical phenotype do not have a predictable molecular basis. Experiments involving resurrected ancestral proteins revealed that historical substitutions have context-dependent effects, indicating that possible adaptive solutions are contingent on prior history. Mutations that produce an adaptive change in one species may represent precluded possibilities in other species because of differences in genetic background.",

author = "Chandrasekhar Natarajan and Hoffmann, {Federico G} and Weber, {Roy E} and Angela Fago and Witt, {Christopher C} and Storz, {Jay F}",

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AU - Natarajan, Chandrasekhar

AU - Hoffmann, Federico G

AU - Weber, Roy E

AU - Fago, Angela

AU - Witt, Christopher C

AU - Storz, Jay F

PY - 2016/10/21

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N2 - To investigate the predictability of genetic adaptation, we examined the molecular basis of convergence in hemoglobin function in comparisons involving 56 avian taxa that have contrasting altitudinal range limits. Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa, but few such changes were attributable to parallel amino acid substitutions at key residues. Thus, predictable changes in biochemical phenotype do not have a predictable molecular basis. Experiments involving resurrected ancestral proteins revealed that historical substitutions have context-dependent effects, indicating that possible adaptive solutions are contingent on prior history. Mutations that produce an adaptive change in one species may represent precluded possibilities in other species because of differences in genetic background.

AB - To investigate the predictability of genetic adaptation, we examined the molecular basis of convergence in hemoglobin function in comparisons involving 56 avian taxa that have contrasting altitudinal range limits. Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa, but few such changes were attributable to parallel amino acid substitutions at key residues. Thus, predictable changes in biochemical phenotype do not have a predictable molecular basis. Experiments involving resurrected ancestral proteins revealed that historical substitutions have context-dependent effects, indicating that possible adaptive solutions are contingent on prior history. Mutations that produce an adaptive change in one species may represent precluded possibilities in other species because of differences in genetic background.

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Predictable convergence in hemoglobin function has unpredictable molecular underpinnings

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