| Title |
Positive selection adaptation of two-domain arginine kinase (AK) from cold seep Vesicomyidae clams
|
|---|---|
| Published in |
Molecular Biology Reports, July 2018
|
| DOI | 10.1007/s11033-018-4227-3 |
| Pubmed ID | |
| Authors |
Xue Kong, Helu Liu, Haibin Zhang |
| Abstract |
Arginine kinase (AK) is an important member of Phosphagen kinases which engage in energy metabolism process, and AKs from cold seep clams may develop an effective mechanism to adapt a special habitat (e.g. low temperature). Three Vesicomyidae clams and seven Veneridae clams (belong to the same Order Veneroida) were chosen to analyze the evolution of two-domain AKs. In the present study, ten two-domain AKs were identified and Neighbor-joining tree showed that AKs were divided into two groups. Branch-site model indicated that two-domain AKs were subjected to strong positive selection (ω2a = 17.5058). 16 positively selective sites were detected and five of them showed posterior probabilities of 0.95 or more. Comparative analysis found that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites were located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae AKs might participate in change of the synergism and in the function of its cold-adapted characteristics. In conclusion, our studies provide evidence of positive Darwinian selection in the two-domain AKs family of Vesicomyidae clams, and may contribute to a better understanding of its adaptation mechanisms to cold seep habitats. |
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| Country | Count | As % |
|---|---|---|
| Unknown | 1 | 100% |
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|---|---|---|
| Scientists | 1 | 100% |
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|---|---|---|
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| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 3 | 75% |
| Student > Master | 1 | 25% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 1 | 25% |
| Earth and Planetary Sciences | 1 | 25% |
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Attention Score in Context
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#20,525,274
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