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Nucleic Acids Research, 1985, Vol. 13, No. 8 2815-2826
© 1985

Articles

Analysis of cDNA and genomic clones coding for the pro{alpha}1 chain of calf Type II collagen

Frank O. Sangiorgi, Virginia Benson-Chanda, Wouter J. de Wet*, Mark E. Sobel+ and Francesco Ramirez

Department of Obstetrics and Gynecology, University of Medicine and Dentistry of New Jersey-Rutgers Medical School Piscataway, NJ 08854, USA *Department of Biochemistry, Potchefstroom University Potchefstroom 2520, South Africa +National Cancer Institute, Laboratory of Pathology, National Institutes of Health Bethesda, MD 20205, USA

Received December 21, 1984. Accepted March 21, 1985.

A bovine cDNA library constructed from fetal cartilage RNA was screened with a pro{alpha}1(II) collagen specific chicken cDNA. A recombinant clone (Bc 7), with an insert of 1 kb, was identified and shown to contain sequences exhibiting 85% homology with the chicken proa{alpha}1(II) collagen C-propeptide. Interspecies comparison strongly suggested that one potential glycosylation site present in the avian C-propeptide is not utilized, since this site is absent in the bovine chain. In addition, two overlapping genomic clones (Pal 3 and Pal 4) were isolated and partially characterized. These clones span 23 kb of DNA and contain approximately 17 kb of the pro{alpha}1(II) calf gene. Sequencing of exon 1 has determined the length of the 3' untranslated region and the exact location of the polyadenylation attachment site.


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[Abstract] [Full Text] [PDF]


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