Nucleotide sequences of complementary deoxyribonucleic acids for the pro.alpha.1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution

Abstract

Nucleotide sequences were determined for two cloned cDNAs encoding for over three-fourths of the pro alpha 1 (I) chain of type I procollagen from man. Comparison with previously published data on amino acid sequences of the alpha 1 (I) chain of type I collagen made it possible to examine mutations in the transcribed products of the gene which have occurred during the evolution of man, calf, rat, mouse, and chick. Comparison of the nucleotide sequences with the corresponding sequences of cDNAs from chick [Fuller, F., & Boedtker, H. (1981) Biochemistry 20, 996] and with cDNAs for the pro alpha 2(I) chain from man [Bernard, M.P., Myers, J. C., Chu, M.-L., Ramirez, F., Eikenberry, E. F., & Prockop, D. J. (1983) Biochemistry 22, 1139] demonstrated that selective pressure during evolution for 250 million or more years acted more strongly on the structure of the pro alpha 1 (I) chain than on the pro alpha 2(I) chain. To improve the reliability of the comparison, the nucleotide sequences were examined with a modification of previous procedures for evaluating mutations in replacement sites and silent sites. The corrected divergence for replacement sites between the alpha 1 (I) chains was 6 +/- 0.8% whereas it was 15 +/- 1.9% for the alpha 2(I) chains. The C-propeptide domain of the pro alpha 1 (I) chain was also highly conserved with a corrected divergence at replacement sites of 5 +/- 0.9%, a value that was not distinguishable from the value previously found for the C-propeptide of the pro alpha 2(I) chain. Therefore, a large part of the structure of both C-propeptides appears to be under selective pressure. Inspection of changes in the C-propeptide of the pro alpha 1 (I) chain suggested that there was a highly conserved region around the carbohydrate attachment site similar to the highly conserved region of 37 amino acids previously found in the C-propeptide of the pro alpha 2(I) chain. Two statistical tests, however, were unable to confirm nonrandom distribution of changes in the C-propeptide of the pro alpha 1(I) chain. The same tests established the presence of a nonrandom distribution in nucleotide changes of the C-propeptide of the pro alpha 2(I) chain. The 3'-noncoding region of the cDNA for pro alpha 1(I) of human type I procollagen showed no homology with the same region in the chick.(ABSTRACT TRUNCATED AT 400 WORDS)

Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

“…3) (7,8,19,(30)(31)(32)(33)(34)(35). The homology of Emfla with fibrillar collagens is evident and a conservation of the general organization of this region is observed.…”

“…Nevertheless, a possible site of cleavage could be the Ala-Glu bond in the sequence Tyr-Arg-Gly-Gln-Ala-Glu-Glu (Fig. 2) by a triplet Gly-Gly-Gly as observed in the a2(I) chain (30) and following a triple helix stabilized by a high imino acid content in the last few triplets as already described for other collagen chains (37). This telopeptide does not contain any lysine residue that could participate in covalent cross-linking, a situation already encountered in the a2(I) chain (30).…”

“…Alignment of portions of the carboxyl propeptide of Emfla, sea urchin COLL1a (19), and human fibrillar collagens (7,8,(30)(31)(32)(33)(34)(35). Computer alignments were done with the sequence analysis program DNAid (28).…”

Expression of a type II collagen gene in the zebrafish embryonic axis

“…The stop codons are in comparable locations in all three species. Despite the collagen Gly-X-Y repeat motif, the sequenced region has much less identity with other collagen genes; for example, 68% with human alpha collagen type I (COLlAl) (Bernard et al, 1983) and 63% with human alpha collagen type I11 (COL3A1) (Janeczko and Ramirez, 1989). While the zebrafish clone is a partial cDNA, encoding the C-terminal one third of the protein (464 amino acids cloned in zebrafish versus 1,418 amino acids in the full-length human protein), this is sufficient for its unambiguous identification as a portion of a zebrafish gene for type I1 collagen; therefore, we call the gene col2al.…”

Preosteoblast Behavior on a Synthetic Calcium Phosphate Scaffold Coated with Cell Derived Matrix

“…47 One unique property of ECM that could assist this approach is its wellconserved structure across species, resulting in minimal rejection of even xenogeneic ECM implants. [48][49][50][51] This property makes it possible to generate ECM from any number of sources to function as a bioactive agent delivery vehicle.…”