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.
Date: 2010
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
MeSH Terms:
  • Alternative Splicing*
  • Amino Acid Motifs/genetics
  • Animals
  • Base Sequence
  • Collagen*/chemistry
  • Collagen*/genetics
  • Collagen*/metabolism
  • Collagen Type III/genetics
  • Collagen Type III/metabolism
  • Collagen Type V/chemistry
  • Collagen Type V/genetics
  • Collagen Type V/metabolism*
  • Extracellular Matrix/genetics
  • Extracellular Matrix/metabolism
  • Genes
  • Humans
  • Procollagen/genetics*
  • Procollagen/metabolism
  • Protein Structure, Tertiary/genetics
  • Zebrafish/genetics
  • Zebrafish/metabolism
PubMed: 20102740 Full text @ Matrix Biol.
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ABSTRACT
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.
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