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To sequence and analyze the 3' coding and noncoding regions of chicken pro-alpha 1(I) and pro-alpha 2(I) collagen mRNAs.

February 17, 1981Biochemistry

Sequence determination and analysis of the 3' region of chicken Pro-.alpha.1(I) and Pro-.alpha.2(I) collagen messenger ribonucleic acids including the carboxy-terminal propeptide sequences

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To sequence and analyze the 3' coding and noncoding regions of chicken pro-alpha 1(I) and pro-alpha 2(I) collagen mRNAs.
Determined DNA sequences from five cDNA clones: three pro-alpha 1 clones (pCg1, pCg26, pCg54) and two pro-alpha 2 clones (pCg13, pCg45).
Deduced amino acid sequences from helical residue 814 through the carboxy-terminal propeptide to the in-phase termination codons, including 3' untranslated regions.
Calculated G+C percentages, CpG (pCG) dinucleotide frequencies, and codon usage preferences across triple-helical and propeptide domains.
Sequenced 1,589 base pairs of pro-alpha 1 and 1,691 base pairs of pro-alpha 2 mRNAs, resolving 201 triple-helical residues and complete C-terminal propeptides (272 residues for pro-alpha 1 and 260 for pro-alpha 2).
Pro-alpha 1 mRNA exhibited higher G+C content (75% helical, 61% C-terminal) than pro-alpha 2 (60% helical, 48% C-terminal), alongside a fivefold higher frequency of pCG dinucleotides.
Identified limited nucleotide homology within helical coding regions despite 50% amino acid conservation at X and Y positions, directly reflecting distinct codon usage patterns.

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Molecular analysis reveals divergent sequence composition and codon usage in chicken procollagen mRNAs, indicating distinct evolutionary adaptations.

Fuller et al. (1981) studied this question.

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Molecular analysis reveals divergent sequence composition and codon usage in chicken procollagen mRNAs, indicating distinct evolutionary adaptations.