期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 115, 期 8, 页码 1865-1870出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1720487115
关键词
hemoglobin; hypoxia; mutation bias; biochemical adaptation; convergence
资金
- Strategic Priority Research Program, Chinese Academy of Sciences [XDB13020300]
- National Science Foundation of China [31630069]
- Key Laboratory of Zoological Systematics and Evolution [O529YX5105]
- NIH [HL087216]
- National Science Foundation [MCB-1517636]
- RII Track-2 [FEC-1736249]
- Danish Council for Independent Research, Natural Sciences [4181-00094]
When different species experience similar selection pressures, the probability of evolving similar adaptive solutions may be influenced by legacies of evolutionary history, such as lineage-specific changes in genetic background. Here we test for adaptive convergence in hemoglobin (Hb) function among high-altitude passerine birds that are native to the Qinghai-Tibet Plateau, and we examine whether convergent increases in Hb-O-2 affinity have a similar molecular basis in different species. We documented that high-altitude parid and aegithalid species from the Qinghai-Tibet Plateau have evolved derived increases in Hb-O-2 affinity in comparison with their closest lowland relatives in East Asia. However, convergent increases in Hb-O-2 affinity and convergence in underlying functional mechanisms were seldom attributable to the same amino acid substitutions in different species. Using ancestral protein resurrection and site-directed mutagenesis, we experimentally confirmed two cases in which parallel substitutions contributed to convergent increases in Hb-O-2 affinity in codistributed high-altitude species. In one case involving the ground tit (Parus humilis) and gray-crested tit (Lophophanes dichrous), parallel amino acid replacements with affinity-enhancing effects were attributable to nonsynonymous substitutions at a CpG dinucleotide, suggesting a possible role for mutation bias in promoting recurrent changes at the same site. Overall, most altitude-related changes in Hb function were caused by divergent amino acid substitutions, and a select few were caused by parallel substitutions that produced similar phenotypic effects on the divergent genetic backgrounds of different species.
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