CLONING AND SEQUENCING OF A PORIFERA PARTIAL CDNA CODING FOR A SHORT-CHAIN COLLAGEN

Collagen is present in Porifera, the lowest multicellular animals, but there is no information available on the primary structure of the collagen chains in this phylum. Developing fresh‐water sponges have been used to extract total RNA in order to study in vitro translation products and to construct a cDNA library. Four translated proteins were collagenase‐sensitive (200 kDa, 160 kDa, 81 kDa and 48 kDa). The cDNA library was screened with a human collagen probe and a clone, EmC4, covering 1.2 kb was isolated. Nucleotide sequencing of EmC4 revealed a conceptual open reading frame coding for 366 amino acids terminated by a stop codon TGA with 103 nucleotides downstream. The presumed translation product encoded contained several domains: a non‐collagenous C‐terminal domain of 156 amino acids with 9 cysteines, an uninterrupted collagenous domain of 171 amino acids, a non‐collagenous domain of 16 amino acids with 3 cysteines and a probably incomplete N‐terminal collagenous domain of 23 amino acids. Comparison with other sequences suggested that this collagen chain might belong to a non‐fibrillar collagen family which evolved into several sub‐families giving rise to nematode cuticular collagens, and type IV collagens. Copyright © 1990, Wiley Blackwell. All rights reserved