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Nucleic Acids Research, 1985, Vol. 13, No. 10 3427-3438
© 1985

Articles

Analysis of the promoter region and the N-propeptide domain of the human pro{alpha}2(I) collagen gene

Leon A. Dickson1, Wouter de Wet2, Maurizio Di Liberto1,3, Dominique Weil3 and Francesco Ramirez3

1Dept. Biochem., Univ. Med. & Dentistry New Jersey, Sch. Osteopath. Med. Piscataway, NJ 08854, USA 2Dept. Biochem., Univ. Potchefstroom Potchefstroom, South Africa 3Dept. Obstet. Gynecol., Univ. Med. & Dentistry New Jersey, Rutgers Med. Sch. Piscataway, NJ 08854, USA

Received March 14, 1985. Accepted April 23, 1985.

We have located the exon coding for the start site of transcription of the human pro{alpha}2(I) collagen gene. Comparison with the homologous region of other fibrillar collagen genes has confirmed the existence of a consensus sequence (CATGTCTA-n-TAGACATG) capable of forming a hairpin secondary structure possibly involved in the regulation of collagen biosynthesis. Sequence comparison of the chronosomal regions at the 5' end of the pro{alpha}1(I) and pro{alpha}2(I) collagen genes failed to identify unique DNA elements potentially mediating comon regulatory siguals. Sequencing of four exons coding for the N-terminal propeptide has determined most of its structure and it has implied the existence of smaller coding units similar to the 11 end 18 bp exons originally described in the avien gene.


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