Collagens are highly preserved proteins in invertebrates and vertebrates. To identify the collagens in urochordates, the total RNAextracted from the pharynx of the ascidian Ciona intestinalis was hybridized with a heterologous probe specific for the echinodermParacentrotus lividus fibrillar type I-like larval collagen. Using this probe, two main bands (i.e. 6 and 2.8 kb mRNA) were observed onNorthern blot hybridization. The cDNA library prepared from poly(A) +RNA extracted from pharyngeal tissue was screened and a cDNAthat specifies a type IX-like collagen was identified. This molecule presents a conceptual open reading frame for a protein containing 734amino acids. In particular, we showed a 1a chain type IX-like collagen characterized by three short triple-helical domains interspersed withfour non-triple-helical sequences, with structural features of fibril-associated collagens with interrupted triple-helices (FACIT) collagens.Northern blot hybridizations indicate a 2.8 kb transcript size. Sequence comparison indicated homology (47.64%, 48.95%) between the typeIX-like collagen of C. intestinalis and mouse and human type IX collagen. In situ hybridization of tunic and pharynx tissues shows thepresence of transcripts in connective tissue cells.
|Numero di pagine||7|
|Rivista||BIOCHIMICA ET BIOPHYSICA ACTA, N. GENE STRUCTURE AND EXPRESSION|
|Stato di pubblicazione||Published - 2002|
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