Artículo

Convergent Evolution of Hemoglobin Function in High-Altitude Andean Waterfowl Involves Limited Parallelism at the Molecular Sequence Level

Chandrasekhar, Natarajan ; Projecto-Garcia, Joana ; Moriyama, Hideaki ; Weber, Roy E. ; Muñoz Fuentes, Violeta ; Green, Andy J. ; Kopuchian, Cecilia Icon; Tubaro, Pablo Luis Icon; Alza, Luis ; Bulgarella, Mariana ; Smith, Matthew M. ; Wilson, Robert E. Icon; Fago, Angela ; McCracken, Kevin G. Icon; Storz, Jay F.

Otros responsables

Fecha

12/2015

Editorial

Public Library of Science

Revista

Plos Genetics

Título del libro

Nombre del evento

Fecha del evento

Institución organizadora

ISSN

1553-7390

eISSN

ISBN

Idioma

Inglés

Tipo del evento

Clasificación temática

Resumen

A fundamental question in evolutionary genetics concerns the extent to which adaptive phenotypic convergence is attributable to convergent or parallel changes at the molecular sequence level. Here we report a comparative analysis of hemoglobin (Hb) function in eight phylogenetically replicated pairs of high- and low-altitude waterfowl taxa to test for convergence in the oxygenation properties of Hb, and to assess the extent to which convergence in biochemical phenotype is attributable to repeated amino acid replacements. Functional experiments on native Hb variants and protein engineering experiments based on site-directed mutagenesis revealed the phenotypic effects of specific amino acid replacements that were responsible for convergent increases in Hb-O2 affinity in multiple high-altitude taxa. In six of the eight taxon pairs, high-altitude taxa evolved derived increases in Hb-O2 affinity that were caused by a combination of unique replacements, parallel replacements (involving identical-by-state variants with independent mutational origins in different lineages), and collateral replacements (involving shared, identical-by-descent variants derived via introgressive hybridization). In genome scans of nucleotide differentiation involving high- and low-altitude populations of three separate species, function-altering amino acid polymorphisms in the globin genes emerged as highly significant outliers, providing independent evidence for adaptive divergence in Hb function. The experimental results demonstrate that convergent changes in protein function can occur through multiple historical paths, and can involve multiple possible mutations. Most cases of convergence in Hb function did not involve parallel substitutions and most parallel substitutions did not affect Hb-O2 affinity, indicating that the repeatability of phenotypic evolution does not require parallelism at the molecular level.

Aprobación

Revisión

Complementado por

Referenciado por

Licencia Creative Commons

Excepto donde se indique lo contrario, la licencia de este ítem se describe como by-nc-sa