Trimeric assembly of collagen XII: effect of deletion of the C-terminal part of the molecule.
The fibril-associated-collagens-with-interrupted-triple-helices (FACITs) are devoid of large C-propeptides like those involved in the trimeric assembly of the fibrillar collagens. Under these conditions, the C-terminal non triple-helical domain (NC1) and the adjacent triple-helical domain (COL1) are likely to be responsible for the trimeric assembly of these collagen molecules. Using a recombinant minigene of one of the FACITs, collagen XII, we show that a deletion covering most of the NC1 domain, except the first seven residues containing a cysteine and constituting the main part of the conserved junction between the COL1 and NC1 domains, does not prevent the formation of trimeric disulfide-bonded assembly of truncated alpha chains. These results suggest that if the non triple-helical NC1 domain is involved in the initial events governing the trimeric assembly, it must be through its amino acid residues participating in the junction. Our data confirm also the results obtained in a previous paper (Mazzorana et al.: J. Biol. Chem. 268:3029-3032, 1993) showing that the formation of disulfide bonds is dependent on hydroxylation and suggesting that the folding of the triple helix (or a part of it) precedes the formation of the disulfide bonds.
Mazzorana
M
M
Institut de Biologie et Chimie des Proteines, Lyon, France.
Giry-Lozinguez
C
C
van der Rest
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D003094:Collagen / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017353:Gene Deletion; D006367:HeLa Cells; D006801:Humans; D006900:Hydroxylation; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes / Q000235:genetics; D017510:Protein Folding; D011995:Recombination, Genetic; D016324:Sequence Tagged Sites
D015345:Oligonucleotide Probes; D003094:Collagen