Characterization of the six zebrafish clade B fibrillar procollagen genes, with evidence for evolutionarily conserved alternative splicing within the pro-α1(V) C-propeptide
| Autor: | Amanda M. Branam, Daniel S. Greenspan, Guorui Huang, Francisco Pelegri, William G. Cole, Richard M. Wenstrup, Guy G. Hoffman |
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| Rok vydání: | 2010 |
| Předmět: |
Amino Acid Motifs
Protein domain Article Animals Humans Clade Molecular Biology Gene Zebrafish Synteny Genetics Base Sequence biology Alternative splicing biology.organism_classification Extracellular Matrix Protein Structure Tertiary Alternative Splicing Procollagen peptidase Collagen Type III Genes Collagen Collagen Type V Procollagen Function (biology) |
| Zdroj: | Matrix Biology. 29:261-275 |
| ISSN: | 0945-053X |
| DOI: | 10.1016/j.matbio.2010.01.006 |
| Popis: | Genes for tetrapod fibrillar procollagen chains can be divided into two clades, A and B, based on sequence homologies and differences in protein domain and gene structures. Although the major fibrillar collagen types I-III comprise only clade A chains, the minor fibrillar collagen types V and XI comprise both clade A chains and the clade B chains pro-alpha1(V), pro-alpha3(V), pro-alpha1(XI) and pro-alpha2(XI), in which defects can underlie various genetic connective tissue disorders. Here we characterize the clade B procollagen chains of zebrafish. We demonstrate that in contrast to the four tetrapod clade B chains, zebrafish have six clade B chains, designated here as pro-alpha1(V), pro-alpha3(V)a and b, pro-alpha1(XI)a and b, and pro-alpha2(XI), based on synteny, sequence homologies, and features of protein domain and gene structures. Spatiotemporal expression patterns are described, as are conserved and non-conserved features that provide insights into the function and evolution of the clade B chain types. Such features include differential alternative splicing of NH(2)-terminal globular sequences and the first case of a non-triple helical imperfection in the COL1 domain of a clade B, or clade A, fibrillar procollagen chain. Evidence is also provided for previously unknown and evolutionarily conserved alternative splicing within the pro-alpha1(V) C-propeptide, which may affect selectivity of collagen type V/XI chain associations in species ranging from zebrafish to human. Data presented herein provide insights into the nature of clade B procollagen chains and should facilitate their study in the zebrafish model system. |
| Databáze: | OpenAIRE |
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