|ZFIN ID: ZDB-PUB-100202-4|
Characterization of the Six Zebrafish Clade B Fibrillar Procollagen Genes, with Evidence for Evolutionarily Conserved Alternative Splicing within the pro-alpha1(V) C-propeptide
Hoffman, G.G., Branam, A.M., Huang, G., Pelegri, F., Cole, W.G., Wenstrup, R.M., and Greenspan, D.S.
|Source:||Matrix biology : journal of the International Society for Matrix Biology 29(4): 261-275 (Journal)|
|Registered Authors:||Greenspan, Daniel S., Pelegri, Francisco|
|Keywords:||Collagen type V/XI, Clade B procollagen chains, Spatiotemporal expression, Intron–exon organization, Alternative splicing, Zebrafish|
|PubMed:||20102740 Full text @ Matrix Biol.|
Hoffman, G.G., Branam, A.M., Huang, G., Pelegri, F., Cole, W.G., Wenstrup, R.M., and Greenspan, D.S. (2010) Characterization of the Six Zebrafish Clade B Fibrillar Procollagen Genes, with Evidence for Evolutionarily Conserved Alternative Splicing within the pro-alpha1(V) C-propeptide. Matrix biology : journal of the International Society for Matrix Biology. 29(4):261-275.
ABSTRACTGenes 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.