Variations in the sequences of BMP2 imply different mechanisms for the evolution of morphological diversity in vertebrates
Autor: | Lihong Yuan, Xueguo Zuo, Shuyi Zhang, Zhe Wang, Paul A. Racey |
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Rok vydání: | 2009 |
Předmět: |
Signal peptide
Physiology Molecular Sequence Data Bone Morphogenetic Protein 2 Sequence alignment Biology Biochemistry Evolution Molecular Phylogenetics Genetics Animals Coding region Amino Acid Sequence Molecular Biology Gene Peptide sequence Phylogeny Mammals Base Sequence fungi Evolution of mammals Protein Structure Tertiary Vertebrates Sequence Alignment Function (biology) |
Zdroj: | Comparative Biochemistry and Physiology Part D: Genomics and Proteomics. 4:100-104 |
ISSN: | 1744-117X |
DOI: | 10.1016/j.cbd.2008.12.002 |
Popis: | Bone morphogenetic protein 2 (BMP2) plays an important role in skeletogenesis, osteoblastic differentiation and limb patterning. Its protein coding region consists of the signal peptide, the pro-domain (that regulates post-translational control of synthesis) and the mature domain (that carries out gene function). This gene has been considered previously to be conserved. By re-analyzing the coding region of BMP2 in 31 species of vertebrates, we found that the mature domain region is indeed conserved in mammals, but not among non-mammalian taxa. Moreover, compared to the mature domain, the signal peptide and pro-domain have experienced dramatic variation in all vertebrates. Six amino acid sites in the pro-domain were identified to be under diversifying Darwinian selection in mammals. These results indicate that the signal peptide and pro-domain of BMP2 may be involved in skeletal poly-morphology during mammal evolution and the mature domain may also contribute to this function in non-mammals. This supports the hypothesis that morphological variations in mammals result mainly from a change in post-translational control of synthesis, whereas in non-mammals they result mainly from gene functional change. |
Databáze: | OpenAIRE |
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