title: Characterization of the six zebrafish clade B fibrillar procollagen genes, with evidence for evolutionarily conserved alternative splicing within the pro-alpha1(V) C-propeptide.
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.
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison, WI 53706, USA.
authors.forename: Guy G
authors.initials: GG
authors.lastname: Hoffman
authors.forename: Amanda M
authors.initials: AM
authors.lastname: Branam
authors.forename: Guorui
authors.initials: G
authors.lastname: Huang
authors.forename: Francisco
authors.initials: F
authors.lastname: Pelegri
authors.forename: William G
authors.initials: WG
authors.lastname: Cole
authors.forename: Richard M
authors.initials: RM
authors.lastname: Wenstrup
authors.forename: Daniel S
authors.initials: DS
authors.lastname: Greenspan
mesh_terms: D017398:Alternative Splicing; D020816:Amino Acid Motifs / Q000235:genetics; D000818:Animals; D001483:Base Sequence; D003094:Collagen / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D024061:Collagen Type III / Q000235:genetics / Q000378:metabolism; D024062:Collagen Type V / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005109:Extracellular Matrix / Q000235:genetics / Q000378:metabolism; D005796:Genes; D006801:Humans; D011347:Procollagen / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D015027:Zebrafish / Q000235:genetics / Q000378:metabolism
chemical_list: D024061:Collagen Type III; D024062:Collagen Type V; D011347:Procollagen; D003094:Collagen